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3ZLN

Crystal structure of BCL-XL in complex with inhibitor (Compound 3)

Functional Information from GO Data
ChainGOidnamespacecontents
A0042981biological_processregulation of apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE H0Y A 1197
ChainResidue
APHE105
AARG139
APHE146
ASO41198
AHOH2112
AHOH2143
ASER106
AASP107
ALEU108
AGLU129
ALEU130
AARG132
AASN136
AGLY138

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1198
ChainResidue
APHE105
ASER106
AARG132
AVAL161
AH0Y1197
AHOH2060

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1199
ChainResidue
ALYS20
AGLU98
AGLU184

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1200
ChainResidue
AASN136
ATRP137
AGLY138
ATYR195

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1201
ChainResidue
AARG91
AGLU92
AEDO1202
AEDO1203

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1202
ChainResidue
ATYR15
AGLN19
APRO180
AGLN183
AGLU184
AEDO1201
AHOH2145

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1203
ChainResidue
ATYR15
AASN175
AASP176
APRO180
AEDO1201
AHOH2145

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 2024-07-10

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