Structure of PDB 4twp Chain A

Receptor sequence
>4twpA (length=266) Species: 9606 (Homo sapiens) [Search protein sequence]
DKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLEVEEFLKEA
AVMKEIKHPNLVQLLGVCTREPPFYIIIEFMTYGNLLDYLRECNRQEVNA
VVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRL
MTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGM
SPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFA
EIHQAFETMFQESSIS
3D structure
PDB4twp Axitinib effectively inhibits BCR-ABL1(T315I) with a distinct binding conformation.
ChainA
Resolution2.4 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) D363 A365 R367 N368 D381 P402
Catalytic site (residue number reindexed from 1) D126 A128 R130 N131 D144 P165
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 AXI A L248 Y253 A269 K271 E316 F317 M318 G321 L370 D381 L16 Y21 A37 K39 E79 F80 M81 G84 L133 D144 MOAD: Ki=100pM
PDBbind-CN: -logKd/Ki=10.00,Ki=100pM
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:4twp, PDBe:4twp, PDBj:4twp
PDBsum4twp
PubMed25686603
UniProtP00519|ABL1_HUMAN Tyrosine-protein kinase ABL1 (Gene Name=ABL1)

[Back to BioLiP]