Structure of PDB 2fo0 Chain A

Receptor sequence
>2fo0A (length=466) Species: 9606 (Homo sapiens) [Search protein sequence]
ARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNH
NGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGI
NGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTL
AELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMK
HKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKH
PNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMAT
QISSAMEYLEKKNFIHRNLAARNCLVGENHLVKVADFGLSRLMTGDTYTA
HAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDL
SQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFET
MFQESSISDEVEKELG
3D structure
PDB2fo0 Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase.
ChainA
Resolution2.27 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) N382 A384 R386 N387 D400 A418
Catalytic site (residue number reindexed from 1) N318 A320 R322 N323 D336 A354
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 P16 A L267 Y272 V275 A288 K290 M309 T334 F336 M337 G340 L389 A399 L203 Y208 V211 A224 K226 M245 T270 F272 M273 G276 L325 A335 BindingDB: IC50=2.8nM
Gene Ontology
Molecular Function
GO:0004672 protein 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:2fo0, PDBe:2fo0, PDBj:2fo0
PDBsum2fo0
PubMed16543148
UniProtP00519|ABL1_HUMAN Tyrosine-protein kinase ABL1 (Gene Name=ABL1)

[Back to BioLiP]