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3SP7

Crystal Structure of Bcl-xL bound to BM903

Functional Information from GO Data
ChainGOidnamespacecontents
A0042981biological_processregulation of apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues30
DetailsBINDING SITE FOR RESIDUE 03B A 210
ChainResidue
APHE0
ATYR101
AALA104
APHE105
AGLU129
ALEU130
AARG132
AASN136
ATRP137
AGLY138
AARG139
AGLN19
AVAL141
AALA142
APHE146
AALA149
APHE191
ATYR195
AASN198
AALA199
AHOH246
AHOH250
ALYS20
AHOH333
AHOH32
AHOH36
AHOH42
AGLU96
APHE97
AARG100

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 211
ChainResidue
AGLU7
AASP11
AHOH243
AHOH317

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 212
ChainResidue
ALYS20
AGLU98
AGLU129
AHOH285
AHOH287
AACT501

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 213
ChainResidue
AGLU124
AHIS177
AGLU193
AACT503

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN A 214
ChainResidue
AGLU184

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 501
ChainResidue
AGLU98
AGLU129
AALA149
AZN212
AHOH285
AHOH301
AHOH329

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 502
ChainResidue
AARG6
ATRP24
ASER28

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 503
ChainResidue
AGLU124
AHIS177
AGLU193
AASN197
AZN213
AHOH323

Functional Information from PROSITE/UniProt
site_idPS01080
Number of Residues19
DetailsBH1 Apoptosis regulator, Bcl-2 family BH1 motif signature. LFrDGv.NWGRIVAFFsFGG
ChainResidueDetails
ALEU130-GLY148

site_idPS01258
Number of Residues12
DetailsBH2 Apoptosis regulator, Bcl-2 family BH2 motif signature. WIqenGGWDtFV
ChainResidueDetails
ATRP181-VAL192

site_idPS01259
Number of Residues15
DetailsBH3 Apoptosis regulator, Bcl-2 family BH3 motif signature. VkqaLReAGDEFELR
ChainResidueDetails
AVAL86-ARG100

site_idPS01260
Number of Residues21
DetailsBH4_1 Apoptosis regulator, Bcl-2 family BH4 motif signature. SNRELVvDFLSYKLSQKGYsW
ChainResidueDetails
ASER4-TRP24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Cleavage; by caspase-1
ChainResidueDetails
ATYR101

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PLK3 => ECO:0000269|PubMed:21840391
ChainResidueDetails
AALA89

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:19917720
ChainResidueDetails
AARG102

222036

PDB entries from 2024-07-03

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