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3ZK6

Crystal structure of Bcl-xL in complex with inhibitor (Compound 2).

Functional Information from GO Data
ChainGOidnamespacecontents
A0042981biological_processregulation of apoptotic process
B0042981biological_processregulation of apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE H1I A 1198
ChainResidue
APHE97
AALA142
ASER145
APHE146
AHOH2026
BPHE97
BALA104
BGLY138
BTYR195
BH1I1198
AARG102
APHE105
ASER106
ALEU108
ALEU130
AASN136
AGLY138
AARG139

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE H1I B 1198
ChainResidue
APHE97
AALA104
ATYR195
AH1I1198
AHOH2026
BARG102
BPHE105
BSER106
BASP107
BLEU108
BTHR109
BGLU129
BLEU130
BASN136
BARG139

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 Residues2
DetailsSITE: Cleavage; by caspase-1
ChainResidueDetails
ATYR101
BTYR101

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PLK3 => ECO:0000269|PubMed:21840391
ChainResidueDetails
AALA89
BALA89

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:19917720
ChainResidueDetails
AARG102
BARG102

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PDB entries from 2025-06-18

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