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3C8F

4Fe-4S-Pyruvate formate-lyase Activating Enzyme with partially disordered AdoMet

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006974biological_processDNA damage response
A0016491molecular_functionoxidoreductase activity
A0030955molecular_functionpotassium ion binding
A0043365molecular_function[formate-C-acetyltransferase]-activating enzyme activity
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A0051604biological_processprotein maturation
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 A 500
ChainResidue
ACYS29
AMET31
ACYS33
ACYS36
ATHR41
ATRP42
AGLY78
AASN106
ALYS131

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MT2 A 501
ChainResidue
AHIS37
AGLY77
AGLY78
AASP104
AASN106
AASP129
AARG166

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGE A 502
ChainResidue
AARG21
ASER69
AHIS100
ALEU125
AMET127
ATRP164

Functional Information from PROSITE/UniProt
site_idPS01087
Number of Residues22
DetailsRADICAL_ACTIVATING Radical activating enzymes signature. GpGiRfitFfqG.ClmrClyChN
ChainResidueDetails
AGLY17-ASN38

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:18852451
ChainResidueDetails
ACYS29
ACYS33
ATYR35
ACYS36
AGLY78
AASP129
AHIS202

218853

PDB entries from 2024-04-24

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