Structure of PDB 6yvy Chain C

Receptor sequence
>6yvyC (length=258) Species: 9606 (Homo sapiens) [Search protein sequence]
STRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCT
SDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSF
LQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV
KLGDFLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKN
NDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLST
ILEEEKAQ
3D structure
PDB6yvy Structure-kinetic relationship reveals the mechanism of selectivity of FAK inhibitors over PYK2.
ChainC
Resolution1.918 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D546 A548 R550 N551 D564
Catalytic site (residue number reindexed from 1) D136 A138 R140 N141 D154
Enzyme Commision number 2.7.10.2: non-specific protein-tyrosine 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 P1E C R426 I428 G429 V436 C502 T503 G505 L553 R16 I18 G19 V26 C92 T93 G95 L143 BindingDB: IC50=3800nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:6yvy, PDBe:6yvy, PDBj:6yvy
PDBsum6yvy
PubMed33497606
UniProtQ05397|FAK1_HUMAN Focal adhesion kinase 1 (Gene Name=PTK2)

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