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1AOR

STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0016625molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor
A0033726molecular_functionaldehyde ferredoxin oxidoreductase activity
A0051536molecular_functioniron-sulfur cluster binding
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0016625molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor
B0033726molecular_functionaldehyde ferredoxin oxidoreductase activity
B0051536molecular_functioniron-sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A 606
ChainResidue
AGLU332
AHIS383
BGLU332
BHIS383

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 607
ChainResidue
AHIS181
AHOH5011
AHOH5012
AHOH5013

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 606
ChainResidue
BHOH5024
BHOH5025
BHOH5026
BHIS181

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 A 608
ChainResidue
ATHR73
AARG76
AARG182
ACYS288
ACYS291
ACYS295
ACYS494
APHE496

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 B 607
ChainResidue
BARG76
BCYS288
BCYS291
BCYS295
BCYS494
BPHE496

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues38
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7878465","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AOR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

258009

PDB entries from 2026-08-12

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