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4QGS

Substrate and cofactor-free form of the Aldehyde Reductase YqhD from E. coli.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0005829cellular_componentcytosol
A0008106molecular_functionalcohol dehydrogenase (NADP+) activity
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0018455molecular_functionalcohol dehydrogenase [NAD(P)+] activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A1990002molecular_functionmethylglyoxal reductase (NADPH) (acetol producing) activity
A1990362molecular_functionbutanol dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AASP194
AHIS198
AHIS267
AHIS281
AHOH636
AHOH743

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 402
ChainResidue
AARG380
AARG23
AILE353
APRO354

Functional Information from PROSITE/UniProt
site_idPS00060
Number of Residues21
DetailsADH_IRON_2 Iron-containing alcohol dehydrogenases signature 2. WaTHmlGHeLTAmhgLdHAqT
ChainResidueDetails
ATRP264-THR284

site_idPS00913
Number of Residues29
DetailsADH_IRON_1 Iron-containing alcohol dehydrogenases signature 1. AVlDpvytytlPprqvAnGvvDAFvhtvE
ChainResidueDetails
AALA173-GLU201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15327949
ChainResidueDetails
AGLY38
AGLY93
ATHR138
AASN147
ALYS160
ATYR179

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15327949, ECO:0007744|PDB:1OJ7
ChainResidueDetails
AASP194
AHIS198
AHIS267
AHIS281

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PDB entries from 2024-07-10

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