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4ID7

ACK1 kinase in complex with the inhibitor cis-3-[8-amino-1-(4-phenoxyphenyl)imidazo[1,5-a]pyrazin-3-yl]cyclobutanol

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 1G0 A 401
ChainResidue
AVAL140
AGLY269
AALA156
ALYS158
AMET181
AILE190
ATHR205
AGLU206
AALA208
ALEU259

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AARG251
AARG275
ATYR284
AGLN287
AARG290

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGDGSFGVVRrGewdapsgktvs.......VAVK
ChainResidueDetails
ALEU132-LYS158

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNLLL
ChainResidueDetails
APHE248-LEU260

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP252

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALEU132
ALYS158

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SRC and autocatalysis => ECO:0000269|PubMed:15308621, ECO:0000269|PubMed:16472662, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20623637, ECO:0000269|PubMed:20979614, ECO:0000269|PubMed:21169560, ECO:0000269|PubMed:21309750, ECO:0007744|PubMed:19369195
ChainResidueDetails
ATYR284

219140

PDB entries from 2024-05-01

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