Structure of PDB 6v74 Chain C

Receptor sequence
>6v74C (length=499) Species: 9606 (Homo sapiens) [Search protein sequence]
IQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLK
EMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVAL
DTKGPEIRTGLIEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVV
EVGSKIYVDDGLISLENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFG
VEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDE
ILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVICATQMLE
SMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIA
REAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEASFKCCSGAIIVLT
KSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQEAW
AEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
3D structure
PDB6v74 Biochemical and structural insights into how amino acids regulate pyruvate kinase muscle isoform 2.
ChainC
Resolution2.32 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R73 R120 K270 T328
Catalytic site (residue number reindexed from 1) R61 R108 K238 T296
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 ASN C T45 G46 N70 R106 H464 Y466 I469 T33 G34 N58 R94 H432 Y434 I437 MOAD: Kd=27uM
BS02 OXL C K270 A293 G295 D296 T328 K238 A261 G263 D264 T296
BS03 FBP C L431 T432 S434 S437 R489 G514 R516 G518 S519 G520 F521 L399 T400 S402 S405 R457 G482 R484 G486 S487 G488 F489
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6v74, PDBe:6v74, PDBj:6v74
PDBsum6v74
PubMed32144209
UniProtP14618|KPYM_HUMAN Pyruvate kinase PKM (Gene Name=PKM)

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