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1HYU

CRYSTAL STRUCTURE OF INTACT AHPF

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
A0005829cellular_componentcytosol
A0008785molecular_functionalkyl hydroperoxide reductase activity
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0045454biological_processcell redox homeostasis
A0050660molecular_functionflavin adenine dinucleotide binding
A0051287molecular_functionNAD binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 800
ChainResidue
AARG430
AARG432

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 801
ChainResidue
ALYS179
AILE437
AHIS438
ASER439

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 900
ChainResidue
AGLN496
AFAD700
AASN257
AHIS347
ACYS348

site_idAC4
Number of Residues33
DetailsBINDING SITE FOR RESIDUE FAD A 700
ChainResidue
AGLY219
AGLY221
APRO222
AALA223
AGLU243
AARG244
AGLY247
AGLN248
AASN257
AGLN288
ASER289
AALA290
AALA321
ATHR322
AGLY323
ACYS345
AGLY487
AASP488
ALYS495
AGLN496
AILE497
AALA500
ACL900
AHOH905
AHOH907
AHOH909
AHOH910
AHOH913
AHOH925
AHOH940
AHOH956
AHOH987
AHOH1071

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
AASP214
AARG357
ATHR478

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1tde
ChainResidueDetails
ACYS345
ACYS348
AASP349

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PDB entries from 2024-05-01

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