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Asym./Biol. Unit (Jmol Viewer)

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Title :   STRUCTURE OF THE PROSTAGLANDIN D SYNTHASE FROM THE PARASITIC NEMATODE ONCHOCERCA VOLVULUS

Authors :   M. Perbandt, J. Hoppner, C. Betzel, E. Liebau

Date :   13 Jul 06 (Deposition) - 17 Jul 07 (Release) - 21 Dec 11 (Revision)

Method :   X-RAY DIFFRACTION

Resolution :   2.00

Chains :   Asym./Biol. Unit : A,B

Keywords :   Prostaglandin Synthase, Glutathione S-Transferase, River Blindness, Onchocerca Volvulus, Immune Modulation, Transferase (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )

Reference :   M. Perbandt, J. Hoppner, C. Burmeister, K. Luersen, C. Betzel, E. Liebau
Structure Of The Extracellular Glutathione S-Transferase Ovgst1 From The Human Pathogenic Parasite Onchocerca Volvulus.
J. Mol. Biol. V. 377 501 2008
PubMed-ID: 18258257 | Reference-DOI: 10.1016/J.JMB.2008.01.029

Molecule 1 - GLUTATHIONE S-TRANSFERASE 1
	Chains	:	A, B
	EC Number	:	2.5.1.18
	Engineered	:	YES
	Expression System	:	ESCHERICHIA COLI
	Expression System Strain	:	BL21 STAR
	Expression System Taxid	:	562
	Expression System Vector	:	PJC20
	Expression System Vector Type	:	PLASMID
	Gene	:	GST1
	Organism Scientific	:	ONCHOCERCA VOLVULUS
	Organism Taxid	:	6282

		1	2
Asymmetric/Biological Unit	:	A	B

Summary Information (see also Sequences/Alignments below)

Asymmetric/Biological Unit (1, 2)

No.	Name	Count	Type	Full Name
1	GSH	2	Ligand/Ion	GLUTATHIONE

Asymmetric Unit (2, 2)

No.	Name	Evidence	Residues	Description
1	AC1	SOFTWARE	TYR A:32 , ARG A:38 , TRP A:63 , LYS A:67 , GLY A:73 , HIS A:74 , VAL A:75 , PRO A:76 , GLU A:87 , SER A:88 , HOH A:523 , HOH A:528 , HOH A:690 , HOH A:728 , GLU B:121	BINDING SITE FOR RESIDUE GSH A 501
2	AC2	SOFTWARE	GLU A:121 , TYR B:32 , ARG B:38 , TRP B:63 , LYS B:67 , GLY B:73 , HIS B:74 , VAL B:75 , GLU B:87 , SER B:88 , HOH B:520 , HOH B:548 , HOH B:635 , HOH B:638	BINDING SITE FOR RESIDUE GSH B 502

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

Asymmetric/Biological Unit

No.	Residues
1	Val A:75	-	Pro A:76
2	Val B:75	-	Pro B:76

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

Asymmetric/Biological Unit (2, 4)

	PROSITE			UniProtKB		PDB
No.	ID	AC	Description	ID	Location	Count	Location
1	GST_NTER	PS50404	Soluble glutathione S-transferase N-terminal domain profile.	GST1_ONCVO	36-113	2	A:26-103 B:26-103
2	GST_CTER	PS50405	Soluble glutathione S-transferase C-terminal domain profile.	GST1_ONCVO	115-235	2	A:105-225 B:105-225

(no "Exon" information available for 2HNL)

Asymmetric/Biological 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:202
 aligned with GST1_ONCVO | P46434 from UniProtKB/Swiss-Prot  Length:235

    Alignment length:202
                                    43        53        63        73        83        93       103       113       123       133       143       153       163       173       183       193       203       213       223       233  
           GST1_ONCVO    34 QMEKYTLTYFNGRGRAEVIRLLFALANVSYEDNRITRDEWKYLKPRTPFGHVPMLNVSGNVLGESHAIELLLGGRFGLLGTNDWEEAKIMAVVLNIDELFQKLIPWTHEKNTTKKAELFRNLSESDVMPFLGRYEKFLKESTTGHIVGNKVSVADLTVFNMLMTLDDEVKLEEYPQLASFVNKIGQMPGIKEWIKKRPKTYF 235
               SCOP domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains 2hnlA01 A:24-99,A:210-225 Glutaredoxin                                      --------------------------------------------------------------------------------------------------------------2hnlA01          CATH domains
               Pfam domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ....eeeeee..hhhhhhhhhhhhhhh...eeeeehhhhhhhhhhhh......eeee..eeeehhhhhhhhhhhhh.....hhhhhhhhhhhhhhhhhhhhhhhhhhhh.hhhhhhhhhhhhhh.hhhhhhhhhhhhhhh...........hhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhh.hhhhhhhhh..... Sec.struct. author
                 SAPs(SNPs) ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE --GST_NTER  PDB: A:26-103 UniProt: 36-113                                       -GST_CTER  PDB: A:105-225 UniProt: 115-235                                                                                 PROSITE
                 Transcript ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 2hnl A  24 QMEKYTLTYFNGRGRAEVIRLLFALANVSYEDNRITRDEWKYLKPRTPFGHVPMLNVSGNVLGESHAIELLLGGRFGLLGTNDWEEAKIMAVVLNIDELFQKLIPWTHEKNTTKKAELFRNLSESDVMPFLGRYEKFLKESTTGHIVGNKVSVADLTVFNMLMTLDDEVKLEEYPQLASFVNKIGQMPGIKEWIKKRPKTYF 225
                                    33        43        53        63        73        83        93       103       113       123       133       143       153       163       173       183       193       203       213       223

Chain B from PDB  Type:PROTEIN  Length:200
 aligned with GST1_ONCVO | P46434 from UniProtKB/Swiss-Prot  Length:235

    Alignment length:200
                                    45        55        65        75        85        95       105       115       125       135       145       155       165       175       185       195       205       215       225       235
           GST1_ONCVO    36 EKYTLTYFNGRGRAEVIRLLFALANVSYEDNRITRDEWKYLKPRTPFGHVPMLNVSGNVLGESHAIELLLGGRFGLLGTNDWEEAKIMAVVLNIDELFQKLIPWTHEKNTTKKAELFRNLSESDVMPFLGRYEKFLKESTTGHIVGNKVSVADLTVFNMLMTLDDEVKLEEYPQLASFVNKIGQMPGIKEWIKKRPKTYF 235
               SCOP domains -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains 2hnlB01 B:26-99,B:210-225 Glutaredoxin                                    --------------------------------------------------------------------------------------------------------------2hnlB01          CATH domains
               Pfam domains -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ..eeeeee..hhhhhhhhhhhhhhh...eeeeehhhhhhhhhhhh......eeee..eeeehhhhhhhhhhhhh.....hhhhhhhhhhhhhhhhhhhhhhhhhhhh.hhhhhhhhhhhhhh.hhhhhhhhhhhhhhhh..........hhhhhhhhhhhhhh........hhhhhhhhhhhhh..hhhhhhhhh..... Sec.struct. author
                 SAPs(SNPs) -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE GST_NTER  PDB: B:26-103 UniProt: 36-113                                       -GST_CTER  PDB: B:105-225 UniProt: 115-235                                                                                 PROSITE
                 Transcript -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 2hnl B  26 EKYTLTYFNGRGRAEVIRLLFALANVSYEDNRITRDEWKYLKPRTPFGHVPMLNVSGNVLGESHAIELLLGGRFGLLGTNDWEEAKIMAVVLNIDELFQKLIPWTHEKNTTKKAELFRNLSESDVMPFLGRYEKFLKESTTGHIVGNKVSVADLTVFNMLMTLDDEVKLEEYPQLASFVNKIGQMPGIKEWIKKRPKTYF 225
                                    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 2HNL)

Asymmetric/Biological Unit

Classes(

)

Architectures( (-)

)

Topologies( (-)

)

Homologous Superfamilies( (-)

)

Organisms( (-)

)

Class: Alpha Beta (26913)

Architecture: 3-Layer(aba) Sandwich (12045)

Topology: Glutaredoxin (620)

Homologous Superfamily: Glutaredoxin (617)

Onchocerca volvulus. Organism_taxid: 6282. (3)

1a	2hnlA01	A:24-99,A:210-225
1b	2hnlB01	B:26-99,B:210-225

(no "Pfam Domain" information available for 2HNL)

Asymmetric/Biological Unit(hide GO term definitions)

Chain A,B (GST1_ONCVO | P46434)

molecular function
	GO:0004364		glutathione transferase activity		Catalysis of the reaction: R-X + glutathione = H-X + R-S-glutathione. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group.
	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.

Asymmetric/Biological Unit
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	Cis Peptide Bonds
		Val A:75 - Pro A:76	[ RasMol ]
		Val B:75 - Pro B:76	[ RasMol ]

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Description

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Ligands, Modified Residues, Ions (1, 2)

Sites (2, 2)

SS Bonds (0, 0)

Cis Peptide Bonds (2, 2)

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SAPs(SNPs)/Variants (0, 0)

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Exons (0, 0)

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