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Title :   COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH ACETAZOLAMIDE

Authors :   S. Huang, T. Hainzl, A. E. Sauer-Eriksson

Date :   27 Oct 11 (Deposition) - 23 Nov 11 (Release) - 28 Mar 12 (Revision)

Method :   X-RAY DIFFRACTION

Resolution :   1.85

Chains :   Asym. Unit : A,B
Biol. Unit 1: A,B  (2x)

Keywords :   Alpha/Beta, Strand Exchange, Lyase-Lyase Inhibitor Complex (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )

Reference :   S. Huang, T. Hainzl, C. Grundstrom, C. Forsman, G. Samuelsson, A. E. Sauer-Eriksson
Structural Studies Of [Beta]-Carbonic Anhydrase From The Green Alga Coccomyxa: Inhibitor Complexes With Anions And Acetazolamide.
Plos One V. 6 28458 2011
PubMed-ID: 22162771 | Reference-DOI: 10.1371/JOURNAL.PONE.0028458

Molecule 1 - CARBONIC ANHYDRASE
	Chains	:	A, B
	EC Number	:	4.2.1.1
	Engineered	:	YES
	Expression System	:	ESCHERICHIA COLI
	Expression System Plasmid	:	PMAL-C2
	Expression System Taxid	:	562
	Expression System Vector Type	:	PLASMID
	Organism Scientific	:	COCCOMYXA SP. PA
	Organism Taxid	:	41892

		1	2
Asymmetric Unit	:	A	B
Biological Unit 1 (2x)	:	A	B

Summary Information (see also Sequences/Alignments below)

Asymmetric Unit (5, 8)

No.	Name	Count	Type	Full Name
1	AZM	2	Ligand/Ion	5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE
2	CL	1	Ligand/Ion	CHLORIDE ION
3	GOL	2	Ligand/Ion	GLYCEROL
4	PO4	1	Ligand/Ion	PHOSPHATE ION
5	ZN	2	Ligand/Ion	ZINC ION

Biological Unit 1 (3, 10)

No.	Name	Count	Type	Full Name
1	AZM	4	Ligand/Ion	5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE
2	CL	-1	Ligand/Ion	CHLORIDE ION
3	GOL	4	Ligand/Ion	GLYCEROL
4	PO4	2	Ligand/Ion	PHOSPHATE ION
5	ZN	-1	Ligand/Ion	ZINC ION

Asymmetric Unit (8, 8)

No.	Name	Evidence	Residues	Description
1	AC1	SOFTWARE	CYS A:47 , HIS A:103 , CYS A:106 , AZM A:229	BINDING SITE FOR RESIDUE ZN A 228
2	AC2	SOFTWARE	CYS B:47 , HIS B:103 , CYS B:106 , AZM B:229	BINDING SITE FOR RESIDUE ZN B 228
3	AC3	SOFTWARE	CYS A:47 , ASP A:49 , HIS A:103 , CYS A:106 , GLY A:107 , ALA A:108 , TRP A:115 , THR A:123 , ZN A:228 , GOL A:231 , HOH A:356 , HOH A:385 , GLN B:38 , PHE B:66 , TYR B:88	BINDING SITE FOR RESIDUE AZM A 229
4	AC4	SOFTWARE	GLN A:38 , PHE A:66 , TYR A:88 , CYS B:47 , ASP B:49 , VAL B:71 , HIS B:103 , CYS B:106 , GLY B:107 , ALA B:108 , ALA B:111 , TRP B:115 , THR B:123 , ZN B:228 , GOL B:230 , HOH B:392	BINDING SITE FOR RESIDUE AZM B 229
5	AC5	SOFTWARE	LYS A:33 , HOH A:296 , LYS B:140 , ARG B:213	BINDING SITE FOR RESIDUE PO4 A 230
6	AC6	SOFTWARE	ASP A:49 , ARG A:51 , ASN A:105 , GLY A:107 , AZM A:229 , HOH A:246 , HOH A:332 , GLY B:36 , GLN B:38 , TYR B:88	BINDING SITE FOR RESIDUE GOL A 231
7	AC7	SOFTWARE	GLY A:36 , GLN A:38 , TYR A:88 , ASP B:49 , ARG B:51 , ASN B:105 , GLY B:107 , AZM B:229	BINDING SITE FOR RESIDUE GOL B 230
8	AC8	SOFTWARE	ARG A:69 , HOH A:359 , ARG B:69 , HOH B:364	BINDING SITE FOR RESIDUE CL A 232

(no "SS Bond" information available for 3UCJ)

(no "Cis Peptide Bond" information available for 3UCJ)

(no "SAP(SNP)/Variant" information available for 3UCJ)

(no "PROSITE Motif" information available for 3UCJ)

(no "Exon" information available for 3UCJ)

Asymmetric Unit

Reformat:	Number of residues per line = ('0' or empty: single-line sequence representation)
	Number of residues per labelling interval =
	UniProt sequence: complete aligned part

Show mapping:	SCOP domains	CATH domains	Pfam domains	Secondary structure (by author)
	SAPs(SNPs)	PROSITE motifs	Exons
	(details for a mapped element are shown in a popup box when the mouse pointer rests over it)

Chain A from PDB  Type:PROTEIN  Length:222
 aligned with Q96554_9CHLO | Q96554 from UniProtKB/TrEMBL  Length:227

    Alignment length:222
                                    15        25        35        45        55        65        75        85        95       105       115       125       135       145       155       165       175       185       195       205       215       225  
         Q96554_9CHLO     6 TADLSPLLEANRKWADECAAKDSTYFSKVAGSQAPEYLYIGCADSRVSPAQLFNMAPGEVFVQRNVGNLVSNKDLNCMSCLEYTVDHLKIKHILVCGHYNCGACKAGLVWHPKTAGVTNLWISDVREVRDKNAAKLHGLSADDAWDKMVELNVEAQVFNVCASPIVQAAWARGQPLSVHGIVYTPGTGLVKELIKPITGMEDAGALLRADLKQHCFFSESLA 227
               SCOP domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ SCOP domains
               CATH domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ CATH domains
               Pfam domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ Pfam domains
         Sec.struct. author ...hhhhhhhhhhhhhhhhhhh...hhhhh......eeeeee.....hhhhhh......eeeeee........hhhhhhhhhhhhhh....eeeeeee..hhhhhhhhhh.....hhhhhhhhhhhhhhhhhhhhhh..hhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhh....eeeeeee......eeeeeeee.hhhhhhhhh..hhhhhhhhhhhh. Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ SAPs(SNPs)
                    PROSITE ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ PROSITE
                 Transcript ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ Transcript
                 3ucj A   6 TADLSPLLEANRKWADECAAKDSTYFSKVAGSQAPEYLYIGCADSRVSPAQLFNMAPGEVFVQRNVGNLVSNKDLNCMSCLEYTVDHLKIKHILVCGHYNCGACKAGLVWHPKTAGVTNLWISDVREVRDKNAAKLHGLSADDAWDKMVELNVEAQVFNVCASPIVQAAWARGQPLSVHGIVYTPGTGLVKELIKPITGMEDAGALLRADLKQHCFFSESLA 227
                                    15        25        35        45        55        65        75        85        95       105       115       125       135       145       155       165       175       185       195       205       215       225

Chain B from PDB  Type:PROTEIN  Length:222
 aligned with Q96554_9CHLO | Q96554 from UniProtKB/TrEMBL  Length:227

    Alignment length:222
                                    15        25        35        45        55        65        75        85        95       105       115       125       135       145       155       165       175       185       195       205       215       225  
         Q96554_9CHLO     6 TADLSPLLEANRKWADECAAKDSTYFSKVAGSQAPEYLYIGCADSRVSPAQLFNMAPGEVFVQRNVGNLVSNKDLNCMSCLEYTVDHLKIKHILVCGHYNCGACKAGLVWHPKTAGVTNLWISDVREVRDKNAAKLHGLSADDAWDKMVELNVEAQVFNVCASPIVQAAWARGQPLSVHGIVYTPGTGLVKELIKPITGMEDAGALLRADLKQHCFFSESLA 227
               SCOP domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ SCOP domains
               CATH domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ CATH domains
               Pfam domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ Pfam domains
         Sec.struct. author ...hhhhhhhhhhhhhhhhhhh...hhhhh......eeeeee.....hhhhhh......eeeeee........hhhhhhhhhhhhhh....eeeeeee..hhhhhhhhhh.....hhhhhhhhhhhhhhhhhhhhhh..hhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhh....eeeeeee......eeeeeeee.hhhhhhhhh..hhhhhhhhhhhh. Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ SAPs(SNPs)
                    PROSITE ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ PROSITE
                 Transcript ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ Transcript
                 3ucj B   6 TADLSPLLEANRKWADECAAKDSTYFSKVAGSQAPEYLYIGCADSRVSPAQLFNMAPGEVFVQRNVGNLVSNKDLNCMSCLEYTVDHLKIKHILVCGHYNCGACKAGLVWHPKTAGVTNLWISDVREVRDKNAAKLHGLSADDAWDKMVELNVEAQVFNVCASPIVQAAWARGQPLSVHGIVYTPGTGLVKELIKPITGMEDAGALLRADLKQHCFFSESLA 227
                                    15        25        35        45        55        65        75        85        95       105       115       125       135       145       155       165       175       185       195       205       215       225

Legend:		→ Mismatch	(orange background)
	-	→ Gap	(green background, '-', border residues have a numbering label)
		→ Modified Residue	(blue background, lower-case, 'x' indicates undefined single-letter code, labelled with number + name)
	x	→ Chemical Group	(purple background, 'x', labelled with number + name, e.g. ACE or NH2)
	extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '\|'

(no "SCOP Domain" information available for 3UCJ)

(no "CATH Domain" information available for 3UCJ)

(no "Pfam Domain" information available for 3UCJ)

Asymmetric Unit(hide GO term definitions)

Chain A,B (Q96554_9CHLO | Q96554)

molecular function
	GO:0004089	carbonate dehydratase activity	Catalysis of the reaction: H2CO3 = CO2 + H2O.
	GO:0016829	lyase activity	Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
	GO:0046872	metal ion binding	Interacting selectively and non-covalently with any metal ion.
	GO:0008270	zinc ion binding	Interacting selectively and non-covalently with zinc (Zn) ions.
biological process
	GO:0015976	carbon utilization	A series of processes that forms an integrated mechanism by which a cell or an organism detects the depletion of primary carbon sources and then activates genes to scavenge the last traces of the primary carbon source and to transport and metabolize alternative carbon sources such as carbon dioxide or carbonic acid. The utilization process begins when the cell or organism detects carbon levels, includes the activation of genes whose products detect, transport or metabolize carbon-containing substances, and ends when carbon is incorporated into the cell or organism's metabolism.

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(no "Cis Peptide Bonds" information available for 3ucj)

Biological Unit
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		Biological Unit 1	[ Jena3D ]

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	Q96554_9CHLO \| Q96554	:	3uck 3ucm 3ucn 3uco

3uck	COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH PHOSPHATE
3ucm	COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH THIOCYANATE
3ucn	COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH AZIDE
3uco	COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH IODIDE

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Ligands, Modified Residues, Ions (5, 8)

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