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4XVG

Crystal structure of Alkylhydroperoxide Reductase Subunit AhpF from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0008785molecular_functionalkyl hydroperoxide reductase activity
A0009321cellular_componentalkyl hydroperoxide reductase complex
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0042744biological_processhydrogen peroxide catabolic process
A0045454biological_processcell redox homeostasis
A0050660molecular_functionflavin adenine dinucleotide binding
A0051287molecular_functionNAD binding
A0071949molecular_functionFAD binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues38
Detailsbinding site for residue FAD A 700
ChainResidue
AGLY219
AGLN248
AILE249
ATHR252
AILE255
AASN257
AGLN288
ASER289
AALA290
AALA321
ATHR322
AGLY221
AGLY323
AALA324
ACYS348
AASN454
AGLY487
AASP488
ALYS495
AGLN496
AILE497
AALA500
APRO222
AHOH810
AHOH834
AHOH874
AHOH875
AHOH876
AHOH879
AHOH882
AHOH897
AHOH950
AALA223
ATYR230
AGLY242
AGLU243
AARG244
AGLY247

Functional Information from PROSITE/UniProt
site_idPS00573
Number of Residues21
DetailsPYRIDINE_REDOX_2 Pyridine nucleotide-disulphide oxidoreductases class-II active site. CphCDGpl..FkgkrVaVIGGGN
ChainResidueDetails
ACYS345-ASN365

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATHR478
AASP214
AARG357

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS354
ALYS53

221051

PDB entries from 2024-06-12

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