Structure of PDB 1opk Chain A

Receptor sequence
>1opkA (length=449) Species: 10090 (Mus musculus) [Search protein sequence]
NLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPS
NYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSI
SLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTL
HYPAPKRNKPTIYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKK
YSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYI
ITEFMTYGNLLDYLRECNRQEVSAVVLLYMATQISSAMEYLEKKNFIHRN
LAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAY
NKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEG
CPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGK
3D structure
PDB1opk Structural basis for the autoinhibition of c-Abl tyrosine kinase
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N382 A384 R386 N387 D400 A418
Catalytic site (residue number reindexed from 1) N300 A302 R304 N305 D318 A336
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 Y272 V275 A288 K290 M309 T334 M337 G340 L389 A399 F401 Y190 V193 A206 K208 M227 T252 M255 G258 L307 A317 F319
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:1opk, PDBe:1opk, PDBj:1opk
PDBsum1opk
PubMed12654251
UniProtP00520|ABL1_MOUSE Tyrosine-protein kinase ABL1 (Gene Name=Abl1)

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