Structure of PDB 2vgg Chain C

Receptor sequence
>2vggC (length=514) Species: 9606 (Homo sapiens) [Search protein sequence]
QQQLPAADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIK
AGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKG
PEIRTGILQGGPESEVELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVR
VVPVGGRIYIDDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPGAQV
DLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIK
IISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGR
CNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETA
KGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGA
VEAAFKCCAAAIIVLTTTGHSAQLLSRYRPRAAVIAVTRSAQAARQVHLC
RGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVTGWR
PGSGYTNIMRVLSI
3D structure
PDB2vgg Structure and Function of Human Erythrocyte Pyruvate Kinase. Molecular Basis of Nonspherocytic Hemolytic Anemia.
ChainC
Resolution2.74 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) R57 R104 K254 T312
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 C L474 T475 T476 T477 S480 R532 G557 R559 P560 G561 S562 G563 Y564 L415 T416 T417 T418 S421 R473 G498 R500 P501 G502 S503 G504 Y505
BS02 PGA C K313 E315 A336 G338 D339 T371 K254 E256 A277 G279 D280 T312
BS03 MN C F287 E315 D339 F228 E256 D280
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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