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4YJ4

Crystal structure of Bcl-xL in complex with the BIM BH3 domain containing Ile155-to-Arg and Glu158-to-phosphoserine mutations

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0042981biological_processregulation of apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue ACT A 201
ChainResidue
AGLU98
AHOH301

site_idAC2
Number of Residues4
Detailsbinding site for residue CL B 201
ChainResidue
AARG6
AASN175
BGLU151
BARG155

site_idAC3
Number of Residues3
Detailsbinding site for residue CL B 202
ChainResidue
AARG132
BGLN150
BARG153

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
DetailsMOD_RES: Phosphoserine; by PLK3 => ECO:0000250|UniProtKB:Q07817
ChainResidueDetails
ASER49

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q07817
ChainResidueDetails
ASER62

227111

PDB entries from 2024-11-06

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