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3SPF

Crystal Structure of Bcl-xL bound to BM501

Functional Information from GO Data
ChainGOidnamespacecontents
A0042981biological_processregulation of apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE B50 A 501
ChainResidue
AHOH48
AGLN160
AGOL212
APHE97
ATYR101
AALA104
APHE105
ALEU108
AGLU129
ALEU130
APHE146

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 209
ChainResidue
ATRP24
ASER25
AVAL155
AGLN160

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 210
ChainResidue
AASN136
AARG139
AGOL212

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 211
ChainResidue
AALA93
APHE97
AARG100
ATYR195

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 212
ChainResidue
AGLU129
ALEU130
AARG139
AGOL210
AB50501

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

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PDB entries from 2025-06-11

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