Structure of PDB 8hms Chain B

Receptor sequence
>8hmsB (length=519) Species: 9606 (Homo sapiens) [Search protein sequence]
IQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLK
EMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVAL
DTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYK
NICKVVEVGSKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLP
GAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKG
KNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKM
MIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLS
GETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEAT
AVGAVEASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQ
AHLYRGIFPVLSKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVL
TGWRPGSGFTNTMRVVPVP
3D structure
PDB8hms Structural and mechanistic insights into cancer patient-derived mutations in Pyruvate Kinase muscle isoform 2
ChainB
Resolution2.1 Å
3D
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
Enzyme Commision number 2.7.10.2: non-specific protein-tyrosine kinase.
2.7.11.1: non-specific serine/threonine protein kinase.
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 OXL B K270 E272 A293 G295 D296 T328 K258 E260 A281 G283 D284 T316
BS02 FBP B L431 T432 K433 S434 S437 W482 R489 G514 R516 G518 S519 G520 F521 L419 T420 K421 S422 S425 W470 R477 G502 R504 G506 S507 G508 F509
BS03 MG B E272 D296 E260 D284
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003723 RNA binding
GO:0003729 mRNA binding
GO:0003824 catalytic activity
GO:0004713 protein tyrosine kinase activity
GO:0004743 pyruvate kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0023026 MHC class II protein complex binding
GO:0030955 potassium ion binding
GO:0045296 cadherin binding
GO:0046872 metal ion binding
Biological Process
GO:0006096 glycolytic process
GO:0006417 regulation of translation
GO:0012501 programmed cell death
GO:0016310 phosphorylation
GO:0032869 cellular response to insulin stimulus
GO:0061621 canonical glycolysis
GO:1903672 positive regulation of sprouting angiogenesis
GO:2000767 positive regulation of cytoplasmic translation
Cellular Component
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005791 rough endoplasmic reticulum
GO:0005829 cytosol
GO:0005929 cilium
GO:0031982 vesicle
GO:0034774 secretory granule lumen
GO:0062023 collagen-containing extracellular matrix
GO:0070062 extracellular exosome
GO:1903561 extracellular vesicle
GO:1904813 ficolin-1-rich granule lumen

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:8hms, PDBe:8hms, PDBj:8hms
PDBsum8hms
PubMed
UniProtP14618|KPYM_HUMAN Pyruvate kinase PKM (Gene Name=PKM)

[Back to BioLiP]