Structure of PDB 4ebv Chain A

Receptor sequence
>4ebvA (length=262) Species: 9606 (Homo sapiens) [Search protein sequence]
SSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNC
TSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRS
FLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC
VKLGDFGLKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQ
GVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKA
QLSTILEEEKAQ
3D structure
PDB4ebv Discovery and characterization of novel allosteric FAK inhibitors.
ChainA
Resolution1.67 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) D546 A548 R550 N551 D564 K583
Catalytic site (residue number reindexed from 1) D137 A139 R141 N142 D155 K159
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 0O7 A L534 L537 H544 R550 N551 L562 G563 D604 M607 C611 L125 L128 H135 R141 N142 L153 G154 D180 M183 C187 MOAD: ic50=0.99uM
PDBbind-CN: -logKd/Ki=5.38,IC50=4.2uM
BindingDB: IC50=4200nM
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4ebv, PDBe:4ebv, PDBj:4ebv
PDBsum4ebv
PubMed22819505
UniProtQ05397|FAK1_HUMAN Focal adhesion kinase 1 (Gene Name=PTK2)

[Back to BioLiP]