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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8CO4

Crystal structure of apo S-nitrosoglutathione reductase from Arabidopsis thalina

Functional Information from GO Data
ChainGOidnamespacecontents
A0004022molecular_functionalcohol dehydrogenase (NAD+) activity
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0009536cellular_componentplastid
A0010286biological_processheat acclimation
A0012501biological_processprogrammed cell death
A0016491molecular_functionoxidoreductase activity
A0044281biological_processsmall molecule metabolic process
A0046292biological_processformaldehyde metabolic process
A0046294biological_processformaldehyde catabolic process
A0046872molecular_functionmetal ion binding
A0048316biological_processseed development
A0051903molecular_functionS-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
A0080007molecular_functionS-nitrosoglutathione reductase (NADH) activity
A0106321molecular_functionS-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity
A0106322molecular_functionS-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity
B0004022molecular_functionalcohol dehydrogenase (NAD+) activity
B0005737cellular_componentcytoplasm
B0005777cellular_componentperoxisome
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0009536cellular_componentplastid
B0010286biological_processheat acclimation
B0012501biological_processprogrammed cell death
B0016491molecular_functionoxidoreductase activity
B0044281biological_processsmall molecule metabolic process
B0046292biological_processformaldehyde metabolic process
B0046294biological_processformaldehyde catabolic process
B0046872molecular_functionmetal ion binding
B0048316biological_processseed development
B0051903molecular_functionS-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
B0080007molecular_functionS-nitrosoglutathione reductase (NADH) activity
B0106321molecular_functionS-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity
B0106322molecular_functionS-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity
C0004022molecular_functionalcohol dehydrogenase (NAD+) activity
C0005737cellular_componentcytoplasm
C0005777cellular_componentperoxisome
C0005829cellular_componentcytosol
C0008270molecular_functionzinc ion binding
C0009536cellular_componentplastid
C0010286biological_processheat acclimation
C0012501biological_processprogrammed cell death
C0016491molecular_functionoxidoreductase activity
C0044281biological_processsmall molecule metabolic process
C0046292biological_processformaldehyde metabolic process
C0046294biological_processformaldehyde catabolic process
C0046872molecular_functionmetal ion binding
C0048316biological_processseed development
C0051903molecular_functionS-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
C0080007molecular_functionS-nitrosoglutathione reductase (NADH) activity
C0106321molecular_functionS-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity
C0106322molecular_functionS-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity
D0004022molecular_functionalcohol dehydrogenase (NAD+) activity
D0005737cellular_componentcytoplasm
D0005777cellular_componentperoxisome
D0005829cellular_componentcytosol
D0008270molecular_functionzinc ion binding
D0009536cellular_componentplastid
D0010286biological_processheat acclimation
D0012501biological_processprogrammed cell death
D0016491molecular_functionoxidoreductase activity
D0044281biological_processsmall molecule metabolic process
D0046292biological_processformaldehyde metabolic process
D0046294biological_processformaldehyde catabolic process
D0046872molecular_functionmetal ion binding
D0048316biological_processseed development
D0051903molecular_functionS-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
D0080007molecular_functionS-nitrosoglutathione reductase (NADH) activity
D0106321molecular_functionS-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity
D0106322molecular_functionS-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity
Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaAGIvesvGegV
ChainResidueDetails
AGLY68-VAL82
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38308388","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Crystal structure and kinetic behavior of alcohol dehydrogenase III /S-nitrosoglutathione reductase from arabidopsis thaliana.","authors":["Crotty J.","Greving M.","Brettschneider S.","Weichsel A.","Wildner G.F.","Vierling E.","Montfort W.R."]}},{"source":"PDB","id":"3UKO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GL4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L0Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CO4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues52
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Crystal structure and kinetic behavior of alcohol dehydrogenase III /S-nitrosoglutathione reductase from arabidopsis thaliana.","authors":["Crotty J.","Greving M.","Brettschneider S.","Weichsel A.","Wildner G.F.","Vierling E.","Montfort W.R."]}},{"source":"PDB","id":"3UKO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GL4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L0Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P06525","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Crystal structure and kinetic behavior of alcohol dehydrogenase III /S-nitrosoglutathione reductase from arabidopsis thaliana.","authors":["Crotty J.","Greving M.","Brettschneider S.","Weichsel A.","Wildner G.F.","Vierling E.","Montfort W.R."]}},{"source":"PDB","id":"3UKO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L0Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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