Structure of PDB 1qpg Chain A Binding Site BS01

Receptor Information
>1qpg Chain A (length=415) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SLSSKLSVQDLDLKDKRVFIRVDFNVPLDGKKITSNQRIVAALPTIKYVL
EHHPRYVVLASHLGQPNGERNEKYSLAPVAKELQSLLGKDVTFLNDCVGP
EVEAAVKASAPGSVILLENLRYHIEEEGSRKVDGQKVKASKEDVQKFRHE
LSSLADVYINDAFGTAHRAHSSMVGFDLPQRAAGFLLEKELKYFGKALEN
PTRPFLAILGGAKVADKIQLIDNLLDKVDSIIIGGGMAFTFKKVLENTEI
GDSIFDKAGAEIVPKLMEKAKAKGVEVVLPVDFIIADAFSADANTKTVTD
KEGIPAGWQGLDNGPESRKLFAATVAKAKTIVWNGPPGVFEFEKFAAGTK
ALLDEVVKSSAAGNTVIIGGGDTATVAKKYGVTDKISHVSTGGGASLELL
EGKELPGVAFLSEKK
Ligand information
Ligand IDMAP
InChIInChI=1S/C10H17N6O12P3.Mg.H/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21;;/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23);;/q;+1;/p-1/t4-,6-,7-,10-;;/m1../s1
InChIKeyQTQJEIANUKJRTB-IDIVVRGQSA-M
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O[Mg])O[P@](=O)(NP(=O)(O)O)O)O)O)N
OpenEye OEToolkits 2.0.7c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O[Mg])OP(=O)(NP(=O)(O)O)O)O)O)N
CACTVS 3.385Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](=O)(O[Mg])O[P](O)(=O)N[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.385Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](=O)(O[Mg])O[P](O)(=O)N[P](O)(O)=O)[C@@H](O)[C@H]3O
FormulaC10 H16 Mg N6 O12 P3
NameMAGNESIUM-5'-ADENYLY-IMIDO-TRIPHOSPHATE
ChEMBL
DrugBank
ZINC
PDB chain1qpg Chain A Residue 450 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1qpg Structure of the R65Q mutant of yeast 3-phosphoglycerate kinase complexed with Mg-AMP-PNP and 3-phospho-D-glycerate.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		G235 G236 N334 P336 G338 V339 F340 E341 G370 G371 D372 T373
Binding residue
(residue number reindexed from 1)		G235 G236 N334 P336 G338 V339 F340 E341 G370 G371 D372 T373
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) R38 K213 G371 G394
Catalytic site (residue number reindexed from 1) R38 K213 G371 G394
Enzyme Commision number 2.7.2.3: phosphoglycerate kinase.
Gene Ontology
Molecular Function
GO:0004618 phosphoglycerate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0043531 ADP binding
GO:0047134 protein-disulfide reductase (NAD(P)H) activity
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0016310 phosphorylation
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0005886 plasma membrane

View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1qpg, PDBe:1qpg, PDBj:1qpg
PDBsum1qpg
PubMed8672447
UniProtP00560|PGK_YEAST Phosphoglycerate kinase (Gene Name=PGK1)

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