Structure of PDB 2vgi Chain D

Receptor sequence
>2vgiD (length=513) Species: 9606 (Homo sapiens) [Search protein sequence]
QQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKE
MIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALD
TKGPEIRTGILESEVELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVRV
VPVGGRIYIDDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPGAQVD
LPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKI
ISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAK
GNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAV
EAAFKCCAAAIIVLTTTGRSAQLLSWYRPRAAVIAVTRSAQAARQVHLCR
GVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVTGWRP
GSGYTNIMRVLSI
3D structure
PDB2vgi Structure and Function of Human Erythrocyte Pyruvate Kinase. Molecular Basis of Nonspherocytic Hemolytic Anemia.
ChainD
Resolution2.87 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R116 R163 K313 T371
Catalytic site (residue number reindexed from 1) R60 R107 K253 T311
Enzyme Commision number 2.7.1.40: pyruvate kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FBP D L474 T475 T476 T477 S480 W525 R532 G557 G561 S562 L414 T415 T416 T417 S420 W465 R472 G497 G501 S502
BS02 PGA D A336 G338 D339 T371 A276 G278 D279 T311
BS03 MN D E315 D339 E255 D279
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:2vgi, PDBe:2vgi, PDBj:2vgi
PDBsum2vgi
PubMed11960989
UniProtP30613|KPYR_HUMAN Pyruvate kinase PKLR (Gene Name=PKLR)

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