Structure of PDB 2vgg Chain B

Receptor sequence
>2vggB (length=483) Species: 9606 (Homo sapiens) [Search protein sequence]
QQQQLPADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIK
AGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKG
PEIRTIVELVKGSQVLVTANTVWVDYPNIVRVVPVGGRIYIDDGLISLVV
VENGGVLGSRKGVNLPGAQDLPGLSEQDVRDLRFGVEHGVDIVFASFVRK
ASDVAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDL
GIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSD
VANAVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEE
LRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGHSAQLLSRYRPR
AAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSI
3D structure
PDB2vgg Structure and Function of Human Erythrocyte Pyruvate Kinase. Molecular Basis of Nonspherocytic Hemolytic Anemia.
ChainB
Resolution2.74 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
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 B L474 T475 T476 T477 S480 R532 G557 R559 G561 S562 Y564 L384 T385 T386 T387 S390 R442 G467 R469 G471 S472 Y474
BS02 PGA B K313 E315 A336 G338 D339 T371 K223 E225 A246 G248 D249 T281
BS03 MN B F287 E315 D339 F197 E225 D249
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

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

[Back to BioLiP]