Structure of PDB 1gpm Chain A Binding Site BS01

Receptor Information
>1gpm Chain A (length=501) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ENIHKHRILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPS
GIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCYGMQTMAMQLGGHVEA
SNEREFGYAQVEVVNDSALVRGIEDALTADGKPLLDVWMSHGDKVTAIPS
DFITVASTESCPFAIMANEEKRFYGVQFHPEVTHTRQGMRMLERFVRDIC
QCEALWTPAKIIDDAVARIREQVGDDKVILGLSGGVDSSVTAMLLHRAIG
KNLTCVFVDNGLLRLNEAEQVLDMFGDHFGLNIVHVPAEDRFLSALAGEN
DPEAKRKIIGRVFVEVFDEEALKLEDVKWLAQGTIYPDVIESAAKMGLVE
PLKELFKDEVRKIGLELGLPYDMLYRHPFPGPGLGVRVLGEVKKEYCDLL
RRADAIFIEELRKADLYDKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRA
VETIDFMTAHWAHLPYDFLGRVSNRIINEVNGISRVVYDISGKPPATIEW
E
Ligand information
Ligand IDPOP
InChIInChI=1S/H4O7P2/c1-8(2,3)7-9(4,5)6/h(H2,1,2,3)(H2,4,5,6)/p-2
InChIKeyXPPKVPWEQAFLFU-UHFFFAOYSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0O[P@@](=O)([O-])O[P@@](=O)(O)[O-]
CACTVS 3.341O[P]([O-])(=O)O[P](O)([O-])=O
ACDLabs 10.04[O-]P(=O)(O)OP([O-])(=O)O
OpenEye OEToolkits 1.5.0OP(=O)([O-])OP(=O)(O)[O-]
FormulaH2 O7 P2
NamePYROPHOSPHATE 2-
ChEMBL
DrugBank
ZINC
PDB chain1gpm Chain A Residue 526 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1gpm The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		S235 G237 V238 D239 S240 K381
Binding residue
(residue number reindexed from 1)		S233 G235 V236 D237 S238 K357
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) G59 C86 Y87 H181 E183 D239 K381
Catalytic site (residue number reindexed from 1) G57 C84 Y85 H179 E181 D237 K357
Enzyme Commision number 6.3.5.2: GMP synthase (glutamine-hydrolyzing).
Gene Ontology
Molecular Function
GO:0003921 GMP synthase activity
GO:0003922 GMP synthase (glutamine-hydrolyzing) activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0042802 identical protein binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006177 GMP biosynthetic process
GO:0006541 glutamine metabolic process
GO:0046037 GMP metabolic process
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1gpm, PDBe:1gpm, PDBj:1gpm
PDBsum1gpm
PubMed8548458
UniProtP04079|GUAA_ECOLI GMP synthase [glutamine-hydrolyzing] (Gene Name=guaA)

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