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5HES

Human leucine zipper- and sterile alpha motif-containing kinase (ZAK, MLT, HCCS-4, MRK, AZK, MLTK) in complex with vemurafenib

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue 032 A 401
ChainResidue
AGLY23
ATYR84
AALA85
AASP92
ACYS150
AASP151
APHE152
AGLY153
AHOH501
AHOH527
APHE27
AVAL30
AALA43
ALYS45
AILE66
AILE80
ATHR82
AGLU83

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO A 402
ChainResidue
AARG63
AASP144
ALYS148
BPRO126

site_idAC3
Number of Residues16
Detailsbinding site for residue 032 B 401
ChainResidue
BGLY23
BPHE27
BVAL30
BALA43
BLYS45
BILE66
BTHR82
BGLU83
BTYR84
BALA85
BASP92
BCYS150
BASP151
BPHE152
BGLY153
BHOH548

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO B 402
ChainResidue
APRO126
BASP144
BLYS148

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P80192, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP133
BASP133

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P80192, ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ACYS22
BCYS22

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:11836244
ChainResidueDetails
ALYS45
BLYS45

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:32289254
ChainResidueDetails
ASER7
BSER7

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15342622, ECO:0000269|PubMed:26999302
ChainResidueDetails
ATPO161
BTPO161

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:15342622, ECO:0000269|PubMed:26999302
ChainResidueDetails
ASER165
BSER165

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER275
BSER275

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:32289254, ECO:0007744|PubMed:18691976
ChainResidueDetails
ASER302
BSER302

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PDB entries from 2024-07-24

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