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4QVE

Crystal structure of Bcl-xL in complex with BID BH3 domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0042981biological_processregulation of apoptotic process
B0005737cellular_componentcytoplasm
B0042981biological_processregulation of apoptotic process
B0043065biological_processpositive regulation of apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IMD B 401
ChainResidue
AALA104
APHE105
AARG165
BGLN92
BHOH513

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. IarhLAqVGDSMDRS
ChainResidueDetails
BILE86-SER100
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 => ECO:0000250|UniProtKB:P70444
ChainResidueDetails
BARG99

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332
ChainResidueDetails
BSER78

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

237423

PDB entries from 2025-06-11

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