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3DOJ

Structure of Glyoxylate reductase 1 from Arabidopsis (AtGLYR1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003858molecular_function3-hydroxybutyrate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0030267molecular_functionglyoxylate reductase (NADPH) activity
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 290
ChainResidue
ALYS25
ASER45
ACYS47
AGLU48
AGLU52
ALYS56

Functional Information from PROSITE/UniProt
site_idPS00895
Number of Residues14
Details3_HYDROXYISOBUT_DH 3-hydroxyisobutyrate dehydrogenase signature. FLGLGiMGkaMSmN
ChainResidueDetails
APHE5-ASN18

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ALYS170

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q49A26
ChainResidueDetails
ATHR95
ALYS238
AGLY4

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895
ChainResidueDetails
AMET1

221051

PDB entries from 2024-06-12

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