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6JUT

Crystal structure of ZAK in complex with compound 6k

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue C9O A 401
ChainResidue
ACYS22
ATYR84
AALA85
AGLY88
ACYS150
AASP151
APHE152
AGLY153
APHE157
AHOH503
AHOH588
AVAL30
AALA43
ALYS45
AALA54
ASER58
APHE68
AILE80
ATHR82

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDLKsrNVVI
ChainResidueDetails
AVAL129-ILE141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P80192, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP133

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P80192, ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ACYS22

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:11836244
ChainResidueDetails
ALYS45

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:32289254
ChainResidueDetails
ASER7

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15342622, ECO:0000269|PubMed:26999302
ChainResidueDetails
ATHR161

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:15342622, ECO:0000269|PubMed:26999302
ChainResidueDetails
ASER165

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER275

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:32289254, ECO:0007744|PubMed:18691976
ChainResidueDetails
ASER302

219869

PDB entries from 2024-05-15

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