Structure of PDB 4mxx Chain A

Receptor sequence
>4mxxA (length=266) Species: 9606 (Homo sapiens) [Search protein sequence]
KDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEA
FLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGK
YLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVTDFG
LARLIEFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMV
NREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLE
DYFTSTEPQYQPGENL
3D structure
PDB4mxx A conserved water-mediated hydrogen bond network defines bosutinib's kinase selectivity.
ChainA
Resolution2.6 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) D386 R388 A390 N391 D404 F424
Catalytic site (residue number reindexed from 1) D130 R132 A134 N135 D148 F157
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 DB8 A L273 A293 I294 K295 E310 V323 T338 Y340 M341 S342 K343 L393 T403 L17 A37 I38 K39 E54 V67 T82 Y84 M85 S86 K87 L137 T147 BindingDB: IC50=3.8nM,Kd=1nM
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:4mxx, PDBe:4mxx, PDBj:4mxx
PDBsum4mxx
PubMed24292070
UniProtP12931|SRC_HUMAN Proto-oncogene tyrosine-protein kinase Src (Gene Name=SRC)

[Back to BioLiP]