Structure of PDB 2g1t Chain A

Receptor sequence
>2g1tA (length=271) Species: 9606 (Homo sapiens) [Search protein sequence]
YDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVE
EFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECN
RQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVAD
FGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWE
IATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPS
DRPSFAEIHQAFETMFQESSI
3D structure
PDB2g1t A SRC-like inactive conformation in the abl tyrosine kinase domain.
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) D363 A365 R367 N368 D381 P402
Catalytic site (residue number reindexed from 1) D132 A134 R136 N137 D150 P171
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 peptide A Q252 H396 A397 G398 A399 K400 F401 P402 L411 L445 Y449 Q21 H165 A166 G167 A168 K169 F170 P171 L180 L214 Y218
BS02 MG A N368 D381 N137 D150
BS03 112 A L248 G250 G251 Q252 V256 A269 K271 F317 M318 N322 R367 N368 L370 L17 G19 G20 Q21 V25 A38 K40 F86 M87 N91 R136 N137 L139
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

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Biological Process
External links
PDB RCSB:2g1t, PDBe:2g1t, PDBj:2g1t
PDBsum2g1t
PubMed16640460
UniProtP00519|ABL1_HUMAN Tyrosine-protein kinase ABL1 (Gene Name=ABL1)

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