Structure of PDB 4m12 Chain A

Receptor sequence
>4m12A (length=264) Species: 9606 (Homo sapiens) [Search protein sequence]
KWVIDPSELTFVQEIGSGQFGLVHLGYWLNKDKVAIKTIREGAMSEEDFI
EEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRTQRGLF
AAETLLGMCLDVCEGMAYLEEACVIHRDLAARNCLVGENQVIKVSDFGMT
RFVLDDQYTSSTGTKFPVKWASPEVFSFSRYSSKSDVWSFGVLMWEVFSE
GKIPYENRSNSEVVEDISTGFRLYKPRLASTHVYQIMNHCWRERPEDRPA
FSRLLRQLAEIAES
3D structure
PDB4m12 Selectively targeting an inactive conformation of interleukin-2-inducible T-cell kinase by allosteric inhibitors.
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D482 A484 R486 N487 D500 P521
Catalytic site (residue number reindexed from 1) D128 A130 R132 N133 D146 P167
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 1YZ A F403 E406 A407 M410 L413 V419 L421 F435 S499 D500 F501 F506 F49 E52 A53 M56 L59 V65 L67 F81 S145 D146 F147 F152 MOAD: Kd=0.9uM
PDBbind-CN: -logKd/Ki=6.05,Kd=0.9uM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0004715 non-membrane spanning protein tyrosine 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:4m12, PDBe:4m12, PDBj:4m12
PDBsum4m12
PubMed24593284
UniProtQ08881|ITK_HUMAN Tyrosine-protein kinase ITK/TSK (Gene Name=ITK)

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