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5VCW

CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN IN COMPLEX WITH Pelitinib

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 Residues13
Detailsbinding site for residue 93J A 401
ChainResidue
ALEU116
AGLN195
AGLN196
APHE240
AHOH510
ALYS139
AVAL171
ALEU185
ATHR187
AGLU188
ACYS190
AGLY191
APRO192

site_idAC2
Number of Residues2
Detailsbinding site for residue SO4 A 402
ChainResidue
AGLN195
AARG272

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO A 403
ChainResidue
AGLN107
AARG112
AARG140

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 404
ChainResidue
AALA203
ASER204
AASN302
AHOH503

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 405
ChainResidue
AARG146
AGLY147
APRO148
ALYS149

site_idAC6
Number of Residues14
Detailsbinding site for residue 93J B 401
ChainResidue
AALA200
BLEU116
BALA137
BLYS139
BVAL171
BLEU185
BTHR187
BGLU188
BCYS190
BGLY191
BPRO192
BGLN196
BPHE240
BHOH507

site_idAC7
Number of Residues2
Detailsbinding site for residue SO4 B 402
ChainResidue
BGLN195
BARG272

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 B 403
ChainResidue
AARG244
BALA203
BSER204
BASN302

site_idAC9
Number of Residues4
Detailsbinding site for residue SO4 B 404
ChainResidue
BGLY147
BPRO148
BLYS149
BASP150

site_idAD1
Number of Residues4
Detailsbinding site for residue SO4 B 405
ChainResidue
BARG81
BGLY309
BGLU310
BHOH506

site_idAD2
Number of Residues1
Detailsbinding site for residue EDO B 406
ChainResidue
BGLU207

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP233
BASP233

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU116
ALYS139
BLEU116
BLYS139

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P30291
ChainResidueDetails
AASN238
AASP251
AGLY253
BASN238
BASP251
BGLY253

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER94
BSER94

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER120
BSER120

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER143
BSER143

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER160
BSER160

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PDB entries from 2024-07-24

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