1gox Summary

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REFINED STRUCTURE OF SPINACH GLYCOLATE OXIDASE AT 2 ANGSTROMS RESOLUTION

The structure was published by Lindqvist, Y., in 1989 in a paper entitled "Refined structure of spinach glycolate oxidase at 2 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1989.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of (S)-2-HYDROXY-ACID OXIDASE, PEROXISOMAL. This molecule has the UniProt identifier P05414 (GOX_SPIOL)search. The sample contained 370 residues which is 100% of the natural sequence. Out of 370 residues 351 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A (S)-2-HYDROXY-ACID OXIDASE, PEROXISOMAL P05414 (1-369) (GOX_SPIOL)search Spinacia oleraceasearch 97% 370 94%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05414 (1 - 369) (S)-2-HYDROXY-ACID OXIDASE, PEROXISOMAL Spinacia oleracea

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P05414) FMN-linked oxidoreductasessearch Aldolase class Isearch PF01070: FMN-dependent dehydrogenasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P05414) medium-chain-(S)-2-hydroxy-acid oxidase activitysearch (S)-2-hydroxy-acid oxidase activitysearch catalytic activitysearch oxidoreductase activitysearch FMN bindingsearch very-long-chain-(S)-2-hydroxy-acid oxidase activitysearch long-chain-(S)-2-hydroxy-long-chain-acid oxidase activitysearch photorespirationsearch oxidative photosynthetic carbon pathwaysearch oxidation-reduction processsearch peroxisomesearch

Chain InterPro annotation
A FMN-dependent dehydrogenasesearch FMN-dependent alpha-hydroxy acid dehydrogenase, active sitesearch Alpha-hydroxy acid dehydrogenase, FMN-dependentsearch Aldolase-type TIM barrelsearch