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5VCZ

CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN IN COMPLEX WITH Bosutinib isomer

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 Residues15
Detailsbinding site for residue XZN A 401
ChainResidue
ALEU116
ACYS190
AGLY191
AGLN196
APHE240
AASP251
AEDO403
AVAL124
AALA137
ALYS139
AGLU157
AVAL171
ALEU185
ATHR187
AGLU188

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 402
ChainResidue
ASER143
APRO144
ASER204
ACYS301
AASN302
AHOH505

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 403
ChainResidue
ATYR121
AXZN401
AEDO404
AHOH539
AHOH546
AHOH555

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO A 404
ChainResidue
ATYR121
AASP251
AEDO403
AHOH501
AHOH558
AHOH577

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 405
ChainResidue
ASER-1
APHE145
AGLY181

site_idAC6
Number of Residues8
Detailsbinding site for residue EDO A 406
ChainResidue
AGLU310
AGLN314
AGLU331
ASER334
AMET338
ALEU356
AVAL358
AHOH658

site_idAC7
Number of Residues4
Detailsbinding site for residue PEG A 407
ChainResidue
ASER114
AARG115
AGLN313
AHOH508

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGHGSYGEVFkVrskedgrl..........YAVK
ChainResidueDetails
ALEU116-LYS139

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LvHlDVKpaNIFL
ChainResidueDetails
ALEU229-LEU241

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
AASP233

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU116
ALYS139

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P30291
ChainResidueDetails
AASN238
AASP251
AGLY253

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER94

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER120

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER143

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER160

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PDB entries from 2024-07-24

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