Structure of PDB 2jkk Chain A

Receptor sequence
>2jkkA (length=258) Species: 9031 (Gallus gallus) [Search protein sequence]
RDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPAMAVAIKTCKNCTSD
SVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQ
VRKFSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSATDCVKL
GDFGLSRLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGV
KNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL
STILEEEK
3D structure
PDB2jkk Crystal Structures of the Fak Kinase in Complex with Tae226 and Related Bis-Anilino Pyrimidine Inhibitors Reveal a Helical Dfg Conformation.
ChainA
Resolution2.0 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 BI9 A I428 A452 L501 C502 G505 N551 L553 D564 L567 I16 A40 L89 C90 G93 N139 L141 D152 L155 MOAD: ic50=6.24nM
PDBbind-CN: -logKd/Ki=8.20,IC50=6.24nM
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:2jkk, PDBe:2jkk, PDBj:2jkk
PDBsum2jkk
PubMed19030106
UniProtQ00944|FAK1_CHICK Focal adhesion kinase 1 (Gene Name=PTK2)

[Back to BioLiP]