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5C3F

Crystal structure of Mcl-1 bound to BID-MM

Functional Information from GO Data
ChainGOidnamespacecontents
A0042981biological_processregulation of apoptotic process
B0005737cellular_componentcytoplasm
B0043065biological_processpositive regulation of apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue GOL A 401
ChainResidue
AARG176
AARG187
AHOH523
AHOH525
AHOH539
AHOH544

site_idAC2
Number of Residues12
Detailsbinding site for residues NLE B 92 and NLE B 96
ChainResidue
BLEU90
BALA91
BVAL93
BGLY94
BASP95
BNLE97
BASP98
BARG99
BSER100
AASP256
BARG88
BHIS89

site_idAC3
Number of Residues12
Detailsbinding site for residues NLE B 96 and NLE B 97
ChainResidue
AVAL216
AASP256
AVAL265
APHE319
BNLE92
BVAL93
BGLY94
BASP95
BASP98
BARG99
BSER100
BILE101

Functional Information from PROSITE/UniProt
site_idPS01080
Number of Residues20
DetailsBH1 Apoptosis regulator, Bcl-2 family BH1 motif signature. VFsDGvtNWGRIVTLIsFGA
ChainResidueDetails
AVAL253-ALA272

site_idPS01258
Number of Residues12
DetailsBH2 Apoptosis regulator, Bcl-2 family BH2 motif signature. WLvkqRGWDgFV
ChainResidueDetails
ATRP305-VAL316

site_idPS01259
Number of Residues15
DetailsBH3 Apoptosis regulator, Bcl-2 family BH3 motif signature. AletLRrVGDGVQRN
ChainResidueDetails
AALA209-ASN223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Cleavage => ECO:0000250|UniProtKB:P70444
ChainResidueDetails
BARG99
ALYS197

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PDB entries from 2024-07-24

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