Structure of PDB 4brx Chain A

Receptor sequence
>4brxA (length=260) Species: 9031 (Gallus gallus) [Search protein sequence]
RDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPAMAVAIKTCKNCTSD
SVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQ
VRKFSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSATDCVKL
GDFGLSRYMLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQ
GVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKA
QLSTILEEEK
3D structure
PDB4brx Synthesis of Novel Diarylamino-1,3,5-Triazine Derivatives as Fak Inhibitors with Anti-Angiogenic Activity.
ChainA
Resolution2.05 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
Catalytic site (residue number reindexed from 1) D134 A136 R138 N139 D152
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 KGW A I428 L501 C502 G505 E506 N551 L553 D564 L567 I16 L89 C90 G93 E94 N139 L141 D152 L155 MOAD: ic50=0.32uM
PDBbind-CN: -logKd/Ki=6.49,IC50=0.32uM
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:4brx, PDBe:4brx, PDBj:4brx
PDBsum4brx
PubMed23845217
UniProtQ00944|FAK1_CHICK Focal adhesion kinase 1 (Gene Name=PTK2)

[Back to BioLiP]