Structure of PDB 2vgb Chain A

Receptor sequence
>2vgbA (length=517) Species: 9606 (Homo sapiens) [Search protein sequence]
QQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKE
MIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALD
TKGPEIRTGILQGGPESEVELVKGSQVLVTVDPAFRTRGNANTVWVDYPN
IVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPG
AQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGH
GIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMM
IGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSG
ETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTA
IGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQV
HLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVT
GWRPGSGYTNIMRVLSI
3D structure
PDB2vgb Structure and Function of Human Erythrocyte Pyruvate Kinase. Molecular Basis of Nonspherocytic Hemolytic Anemia.
ChainA
Resolution2.73 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 K257 T315
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 A T475 T476 T477 S480 R532 G557 R559 P560 G561 S562 G563 Y564 T419 T420 T421 S424 R476 G501 R503 P504 G505 S506 G507 Y508
BS02 PGA A E315 A336 G338 D339 T371 E259 A280 G282 D283 T315
BS03 MN A E315 D339 E259 D283
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:2vgb, PDBe:2vgb, PDBj:2vgb
PDBsum2vgb
PubMed11960989
UniProtP30613|KPYR_HUMAN Pyruvate kinase PKLR (Gene Name=PKLR)

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