Structure of PDB 6ttf Chain A

Receptor sequence
>6ttfA (length=514) Species: 9606 (Homo sapiens) [Search protein sequence]
LHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEMIKS
GMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGP
EIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKV
VEVGSKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVD
LPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKI
ISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAK
GDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAV
EASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYR
GIFPVLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRP
GSGFTNTMRVVPVP
3D structure
PDB6ttf Fragment-based drug discovery using cryo-EM.
ChainA
Resolution3.2 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) R56 R103 K253 T311
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 LZ2 A F26 L353 I389 Q393 E397 F9 L336 I372 Q376 E380
BS02 FBP A L431 T432 K433 S434 S437 W482 R489 G514 R516 G518 S519 G520 F521 L414 T415 K416 S417 S420 W465 R472 G497 R499 G501 S502 G503 F504
BS03 LZ2 A L27 M30 L10 M13
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:6ttf, PDBe:6ttf, PDBj:6ttf
PDBsum6ttf
PubMed31877353
UniProtP14618|KPYM_HUMAN Pyruvate kinase PKM (Gene Name=PKM)

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