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2J51

Crystal structure of Human STE20-like kinase bound to 5-Amino-3-((4-(aminosulfonyl)phenyl)amino) -N-(2,6-difluorophenyl)-1H-1,2,4-triazole- 1-carbothioamide

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 Residues2
DetailsBINDING SITE FOR RESIDUE SCN A1313
ChainResidue
AARG242
ALYS249

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A1309
ChainResidue
AHIS147
APRO211
ATYR214
AVAL218
ATHR282
ATHR283
AEDO1311

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A1310
ChainResidue
AVAL134
ALYS137
AGLN138
AVAL294
ASER296
AASN297
AEDO1312

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A1311
ChainResidue
AHIS147
ALYS150
AASP209
AEDO1309

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A1312
ChainResidue
AASN90
AASP168
AEDO1310
AHOH2050

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE DKI A1314
ChainResidue
ALEU40
AVAL48
AALA61
AILE108
AGLU109
APHE110
ACYS111
AGLY114
AGLY159
AASN160
ALEU162
AHOH2151

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGDGAFGKVYkAqnketsvl..........AAAK
ChainResidueDetails
ALEU40-LYS63

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKagNILF
ChainResidueDetails
AILE151-PHE163

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP155

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU40
ALYS63

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR10

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O54988
ChainResidueDetails
ATHR183

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER189

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP155
AGLY159

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP155
ALYS157

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP155
ATHR193
ALYS157

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP155
AASN160
ALYS157

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PDB entries from 2024-07-24

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