1ea0 Summary



The structure was published by Binda, C., Bossi, R.T., Wakatsuki, S., et al., Curti, B., Vanoni, M.A., and Mattevi, A., in 2000 in a paper entitled "Cross-Talk and Ammonia Channeling between Active Centers in the Unexpected Domain Arrangement of Glutamate Synthase" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 2000.

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

This PDB entry contains multiple copies of the structure of GLUTAMATE SYNTHASE [NADPH] LARGE CHAIN.

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 GLUTAMATE SYNTHASE [NADPH] LARGE CHAIN Q05755 (37-1515) (GLTB_AZOBR)search Azospirillum brasilensesearch 97% 1479 98%
B GLUTAMATE SYNTHASE [NADPH] LARGE CHAIN Q05755 (37-1515) (GLTB_AZOBR)search Azospirillum brasilensesearch 97% 1479 98%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q05755 (37 - 1515) GLUTAMATE SYNTHASE [NADPH] LARGE CHAIN Azospirillum brasilense

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (Q05755) Alpha subunit of glutamate synthase, C-terminal domainsearch, FMN-linked oxidoreductasessearch, Class II glutamine amidotransferasessearch Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1search, Aldolase class Isearch, Pectate Lyase C-likesearch PF00310: Glutamine amidotransferases class-IIsearch, PF01493: GXGXG motifsearch, PF01645: Conserved region in glutamate synthasesearch, PF04898: Glutamate synthase central domainsearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (Q05755) glutamate biosynthetic processsearch metabolic processsearch nitrogen compound metabolic processsearch oxidation-reduction processsearch cellular amino acid biosynthetic processsearch L-glutamate biosynthetic processsearch glutamine metabolic processsearch glutamate synthase activitysearch oxidoreductase activity, acting on the CH-NH2 group of donorssearch catalytic activitysearch oxidoreductase activitysearch 3 iron, 4 sulfur cluster bindingsearch metal ion bindingsearch iron-sulfur cluster bindingsearch glutamate synthase (NADPH) activitysearch

Chain InterPro annotation
A, B Class II glutamine amidotransferase domainsearch Glutamate synthase, alpha subunit, C-terminalsearch Glutamate synthase domainsearch Glutamate synthase, central-Nsearch Aldolase-type TIM barrelsearch Glutamine amidotransferase type 2 domainsearch Nucleophile aminohydrolases, N-terminalsearch