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3EQP

Crystal Structure of Ack1 with compound T95

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 Residues16
DetailsBINDING SITE FOR RESIDUE T95 B 1
ChainResidue
AASP383
BALA208
BGLY211
BARG256
BASN257
BLEU259
BHOH398
BHOH430
BLEU132
BGLY133
BVAL140
BALA156
BLYS158
BGLU177
BILE190
BTHR205

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 393
ChainResidue
BARG216
BHIS220
BARG263

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE T95 A 1
ChainResidue
ALEU132
AVAL140
AALA156
ALYS158
AGLU177
AILE190
ATHR205
AALA208
APRO209
AGLY211
AARG256
AASN257
ALEU259
AHOH396

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGDGSFGVVRrGewdapsgktvs.......VAVK
ChainResidueDetails
BLEU132-LYS158

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNLLL
ChainResidueDetails
BPHE248-LEU260

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by SRC and autocatalysis","evidences":[{"source":"PubMed","id":"15308621","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16472662","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20333297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20623637","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20979614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21169560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21309750","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG256
BASP252

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG256
AASP252

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BALA254
BASP252

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA254
AASP252

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BALA254
BASN257
BASP252

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA254
AASN257
AASP252

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PDB entries from 2025-12-10

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