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1U46

Crystal Structure of the Unphosphorylated Kinase Domain of the Tyrosine Kinase ACK1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 1
ChainResidue
BARG251
BMET286
BGLN287
BARG290
BHOH480

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 Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP252
BASP252

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ALEU132
ALYS158
BLEU132
BLYS158

site_idSWS_FT_FI3
Number of Residues2
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
BTYR284

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG256
AASP252

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG256
BASP252

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA254
AASP252

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BALA254
BASP252

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA254
AASN257
AASP252

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BALA254
BASN257
BASP252

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PDB entries from 2024-07-24

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