Structure of PDB 2g1t Chain C

Receptor sequence

>2g1tC (length=276) Species: 9606 (Homo sapiens) [Search protein sequence]

YDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVE
EFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECN
RQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVAD
FGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWE
IATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPS
DRPSFAEIHQAFETMFQESSISDEVE

3D structure

PDB

2g1t A SRC-like inactive conformation in the abl tyrosine kinase domain.

Chain

Resolution

1.8 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)
BS01	peptide	C	Q252 H396 A397 G398 A399 K400 F401 P402 I403 L411 L445 Y449	Q21 H165 A166 G167 A168 K169 F170 P171 I172 L180 L214 Y218
BS02	MG	C	N368 D381	N137 D150
BS03	112	C	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

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Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:2g1t, PDBe:2g1t, PDBj:2g1t
PDBsum	2g1t
PubMed	16640460
UniProt	P00519\|ABL1_HUMAN Tyrosine-protein kinase ABL1 (Gene Name=ABL1)

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