2ZTK - JenaLib

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Biological Unit 1 (Jmol Viewer)

Biol. Unit 1 - sites (Jmol Viewer)

Title :   CRYSTAL STRUCTURE OF HOMOCITRATE SYNTHASE FROM THERMUS THERMOPHILUS COMPLEXED WITH HOMOCITRATE

Authors :   T. Okada, T. Tomita, T. Kuzuyama, M. Nishiyama

Date :   06 Oct 08 (Deposition) - 13 Oct 09 (Release) - 25 Jan 12 (Revision)

Method :   X-RAY DIFFRACTION

Resolution :   1.96

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

Keywords :   (Beta/Alpha)8 Tim Barrel, Product Complex, Amino-Acid Biosynthesis, Lysine Biosynthesis, Transferase (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )

Reference :   T. Okada, T. Tomita, A. P. Wulandari, T. Kuzuyama, M. Nishiyama
Mechanism Of Substrate Recognition And Insight Into Feedbac Inhibition Of Homocitrate Synthase From Thermus Thermophilu
J. Biol. Chem. V. 285 4195 2010
PubMed-ID: 19996101 | Reference-DOI: 10.1074/JBC.M109.086330

Molecule 1 - HOMOCITRATE SYNTHASE
	Chains	:	A
	EC Number	:	2.3.3.14
	Engineered	:	YES
	Expression System	:	ESCHERICHIA COLI
	Expression System Plasmid	:	PET-26B(+)
	Expression System Strain	:	BL21 RIL-CODONPLUS (DE3)
	Expression System Taxid	:	562
	Expression System Vector Type	:	PLASMID
	Gene	:	HCS
	Organism Scientific	:	THERMUS THERMOPHILUS
	Organism Taxid	:	262724
	Strain	:	HB27

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

Summary Information (see also Sequences/Alignments below)

Asymmetric Unit (2, 2)

No.	Name	Count	Type	Full Name
1	CU	1	Ligand/Ion	COPPER (II) ION
2	HCA	1	Ligand/Ion	3-HYDROXY-3-CARBOXY-ADIPIC ACID

Biological Unit 1 (1, 2)

No.	Name	Count	Type	Full Name
1	CU	-1	Ligand/Ion	COPPER (II) ION
2	HCA	2	Ligand/Ion	3-HYDROXY-3-CARBOXY-ADIPIC ACID

Asymmetric Unit (2, 2)

No.	Name	Evidence	Residues	Description
1	AC1	SOFTWARE	ARG A:12 , GLU A:13 , GLN A:16 , HIS A:72 , LEU A:94 , ARG A:133 , SER A:135 , GLU A:137 , ALA A:164 , THR A:166 , HIS A:195 , HIS A:197 , HIS A:292 , CU A:384 , HOH A:435 , HOH A:547	BINDING SITE FOR RESIDUE HCA A 383
2	AC2	SOFTWARE	GLU A:13 , HIS A:195 , HIS A:197 , HCA A:383 , HOH A:547	BINDING SITE FOR RESIDUE CU A 384

(no "SS Bond" information available for 2ZTK)

Asymmetric Unit

No.	Residues
1	Met A:1	-	Arg A:2

(no "SAP(SNP)/Variant" information available for 2ZTK)

Asymmetric Unit (3, 3)

	PROSITE			UniProtKB		PDB
No.	ID	AC	Description	ID	Location	Count	Location
1	PYR_CT	PS50991	Pyruvate carboxyltransferase domain.	HOSC_THET2	4-259	1	A:4-259
2	AIPM_HOMOCIT_SYNTH_1	PS00815	Alpha-isopropylmalate and homocitrate synthases signature 1.	HOSC_THET2	11-27	1	A:11-27
3	AIPM_HOMOCIT_SYNTH_2	PS00816	Alpha-isopropylmalate and homocitrate synthases signature 2.	HOSC_THET2	192-205	1	A:192-205

Biological Unit 1 (3, 6)

	PROSITE			UniProtKB		PDB
No.	ID	AC	Description	ID	Location	Count	Location
1	PYR_CT	PS50991	Pyruvate carboxyltransferase domain.	HOSC_THET2	4-259	2	A:4-259
2	AIPM_HOMOCIT_SYNTH_1	PS00815	Alpha-isopropylmalate and homocitrate synthases signature 1.	HOSC_THET2	11-27	2	A:11-27
3	AIPM_HOMOCIT_SYNTH_2	PS00816	Alpha-isopropylmalate and homocitrate synthases signature 2.	HOSC_THET2	192-205	2	A:192-205

(no "Exon" information available for 2ZTK)

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
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Chain A from PDB  Type:PROTEIN  Length:312
 aligned with HOSC_THET2 | O87198 from UniProtKB/Swiss-Prot  Length:376

    Alignment length:320
                                    10        20        30        40        50        60        70        80        90       100       110       120       130       140       150       160       170       180       190       200       210       220       230       240       250       260       270       280       290       300       310       320
           HOSC_THET2     1 MREWKIIDSTLREGEQFEKANFSTQDKVEIAKALDEFGIEYIEVTTPVASPQSRKDAEVLASLGLKAKVVTHIQCRLDAAKVAVETGVQGIDLLFGTSKYLRAAHGRDIPRIIEEAKEVIAYIREAAPHVEVRFSAEDTFRSEEQDLLAVYEAVAPYVDRVGLADTVGVATPRQVYALVREVRRVVGPRVDIEFHGHNDTGCAIANAYEAIEAGATHVDTTILGIGERNGITPLGGFLARMYTLQPEYVRRKYKLEMLPELDRMVARMVGVEIPFNNYITGETAFSHKAGMHLKAIYINPEAYEPYPPEVFGVKRKLIIA 320
               SCOP domains -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains -----------HMGL-like-2ztkA01 A:12-245                                                                                                                                                                                                                --------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ....eeeeeeehhhhhh.....hhhhhhhhhhhhhhhh..eeee.....hhhhhhhhhhhhh.....eeeeeee.hhhhhhhhhhh...eeeeee..--------..hhhhhhhhhhhhhhhhhhhh...eeeeee......hhhhhhhhhhhhhhhh.eeeeee.....hhhhhhhhhhhhhhhhh...eeeeee.....hhhhhhhhhhhh...eeeehhhhh.......hhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhh...............ee.hhhhhhhhhhhhhhhh..hhhhhh...ee... Sec.struct. author
                 SAPs(SNPs) -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                PROSITE (1) ---PYR_CT  PDB: A:4-259 UniProt: 4-259                                                                                                                                                                                                                             ------------------------------------------------------------- PROSITE (1)
                PROSITE (2) ----------AIPM_HOMOCIT_SYNT--------------------------------------------------------------------------------------------------------------------------------------------------------------------AIPM_HOMOCIT_S------------------------------------------------------------------------------------------------------------------- PROSITE (2)
                 Transcript -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 2ztk A   1 MREWKIIDSTLREGEQFEKANFSTQDKVEIAKALDEFGIEYIEVTTPVASPQSRKDAEVLASLGLKAKVVTHIQCRLDAAKVAVETGVQGIDLLFGT--------GRDIPRIIEEAKEVIAYIREAAPHVEVRFSAEDTFRSEEQDLLAVYEAVAPYVDRVGLADTVGVATPRQVYALVREVRRVVGPRVDIEFHGHNDTGCAIANAYEAIEAGATHVDTTILGIGERNGITPLGGFLARMYTLQPEYVRRKYKLEMLPELDRMVARMVGVEIPFNNYITGETAFSHKAGMHLKAIYINPEAYEPYPPEVFGVKRKLIIA 320
                                    10        20        30        40        50        60        70        80        90      |  -     | 110       120       130       140       150       160       170       180       190       200       210       220       230       240       250       260       270       280       290       300       310       320
                                                                                                                           97      106

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 2ZTK)

(no "CATH Domain" information available for 2ZTK)

Asymmetric Unit

Clans(

)

Families(

)

Organisms( (-)

)

Clan: TIM_barrel (694)

Family: HMGL-like (13)

Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) (3)

HMGL-like-2ztkA01

A:12-245

Asymmetric Unit(hide GO term definitions)

Chain A (HOSC_THET2 | O87198)

molecular function
	GO:0003824	catalytic activity	Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
	GO:0004410	homocitrate synthase activity	Catalysis of the reaction: 2-oxoglutarate + acetyl-CoA + H(2)O = CoA + H(+) + homocitrate.
	GO:0016740	transferase activity	Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
	GO:0046912	transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer	Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor), with the acyl group being converted into alkyl on transfer.
biological process
	GO:0019752	carboxylic acid metabolic process	The chemical reactions and pathways involving carboxylic acids, any organic acid containing one or more carboxyl (COOH) groups or anions (COO-).
	GO:0008652	cellular amino acid biosynthetic process	The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
	GO:0009085	lysine biosynthetic process	The chemical reactions and pathways resulting in the formation of lysine, 2,6-diaminohexanoic acid.
	GO:0019878	lysine biosynthetic process via aminoadipic acid	The chemical reactions and pathways resulting in the formation of lysine by the aminoadipic pathway.
cellular component
	GO:0005737	cytoplasm	All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Asymmetric Unit
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	Ligands, Modified Residues, Ions
		CU	[ RasMol \| Jena3D ]	+environment [ RasMol \| Jena3D ]
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	Sites
		AC1	[ RasMol ]	+environment [ RasMol ]
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	Cis Peptide Bonds
		Met A:1 - Arg A:2	[ RasMol ]

Biological Unit
	Complete Structure
		Biological Unit 1	[ Jena3D ]

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	2ztk
		Family and Domain Information	:	ProDom \| SYSTERS
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	2.3.3.14
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	HOSC_THET2 \| O87198	:	2ztj 2zyf 3a9i

Description

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Ligands, Modified Residues, Ions (2, 2)

Sites (2, 2)

SS Bonds (0, 0)

Cis Peptide Bonds (1, 1)

Sequence-Structure Mapping

SAPs(SNPs)/Variants (0, 0)

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Exons (0, 0)

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