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3SFZ

Crystal structure of full-length murine Apaf-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0001822biological_processkidney development
A0001843biological_processneural tube closure
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006915biological_processapoptotic process
A0007420biological_processbrain development
A0007584biological_processresponse to nutrient
A0008656molecular_functioncysteine-type endopeptidase activator activity involved in apoptotic process
A0010659biological_processcardiac muscle cell apoptotic process
A0030154biological_processcell differentiation
A0030900biological_processforebrain development
A0031072molecular_functionheat shock protein binding
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0042981biological_processregulation of apoptotic process
A0043293cellular_componentapoptosome
A0043531molecular_functionADP binding
A0051402biological_processneuron apoptotic process
A0070059biological_processintrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
A0071560biological_processcellular response to transforming growth factor beta stimulus
A0097190biological_processapoptotic signaling pathway
A0097193biological_processintrinsic apoptotic signaling pathway
A1902510biological_processregulation of apoptotic DNA fragmentation
A2001235biological_processpositive regulation of apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP A 1250
ChainResidue
APRO123
AVAL162
APRO321
ALEU322
ASER325
APHE425
AHIS438
AHOH1339
AILE125
AVAL127
AARG129
AALA156
AGLY157
AGLY159
ALYS160
ASER161

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GBL A 1251
ChainResidue
ASER387
ATHR446
ALEU453
AHIS457

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GBL A 1252
ChainResidue
AASP191
AHIS521
AHIS524
AALA528

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GBL A 1253
ChainResidue
ALYS189
AASP191

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GBL A 1254
ChainResidue
AASN551
ACYS569
ATYR1215
AASN1217

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GBL A 1255
ChainResidue
ALEU651
AASP652

Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. IATCsaDkKVKIWDS
ChainResidueDetails
AILE672-SER686
ALEU716-LEU730
ALEU758-VAL772
ALEU1142-VAL1156

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY154

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AARG265

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PDB entries from 2024-07-24

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