Structure of PDB 2vgg Chain B Binding Site BS03

Receptor Information
>2vgg Chain B (length=483) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QQQQLPADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIK
AGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKG
PEIRTIVELVKGSQVLVTANTVWVDYPNIVRVVPVGGRIYIDDGLISLVV
VENGGVLGSRKGVNLPGAQDLPGLSEQDVRDLRFGVEHGVDIVFASFVRK
ASDVAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDL
GIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSD
VANAVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEE
LRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGHSAQLLSRYRPR
AAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSI
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain2vgg Chain B Residue 587 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2vgg Structure and Function of Human Erythrocyte Pyruvate Kinase. Molecular Basis of Nonspherocytic Hemolytic Anemia.
Resolution2.74 Å
Binding residue
(original residue number in PDB)		F287 E315 D339
Binding residue
(residue number reindexed from 1)		F197 E225 D249
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R116 R163 K313 T371
Catalytic site (residue number reindexed from 1) R57 R104 K223 T281
Enzyme Commision number 2.7.1.40: pyruvate kinase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004743 pyruvate kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0030955 potassium ion binding
GO:0046872 metal ion binding
GO:0048029 monosaccharide binding
Biological Process
GO:0001666 response to hypoxia
GO:0006096 glycolytic process
GO:0007584 response to nutrient
GO:0009749 response to glucose
GO:0010038 response to metal ion
GO:0016310 phosphorylation
GO:0032869 cellular response to insulin stimulus
GO:0033198 response to ATP
GO:0042866 pyruvate biosynthetic process
GO:0051591 response to cAMP
GO:0071872 cellular response to epinephrine stimulus
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2vgg, PDBe:2vgg, PDBj:2vgg
PDBsum2vgg
PubMed11960989
UniProtP30613|KPYR_HUMAN Pyruvate kinase PKLR (Gene Name=PKLR)

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