Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3QGW

Crystal Structure of ITK kinase bound to an inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PQC A 1
ChainResidue
AILE369
BVAL366
AALA389
APHE435
AGLU436
APHE437
AMET438
ACYS442
ALEU489
BPHE365

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE L7A B 1
ChainResidue
BALA389
BLYS391
BPHE435
BGLU436
BPHE437
BMET438
BGLY441
BLEU489
BSER499
BASP500

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues23
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGQFGLVHlGywlnkdk...........VAIK
ChainResidueDetails
AILE369-LYS391

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. VIHrDLAARNCLV
ChainResidueDetails
AVAL478-VAL490

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP482
BASP482

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BILE369
BLYS391
AILE369
ALYS391

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by LCK => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR512
BTYR512

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ASER565
BSER565

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon