1psd Summary

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THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE

The structure was published by Schuller, D.J., Grant, G.A., and Banaszak, L.J., in 1995 in a paper entitled "The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.75 Å and deposited in 1995.

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

This PDB entry contains multiple copies of the structure of D-3-PHOSPHOGLYCERATE DEHYDROGENASE (PHOSPHOGLYCERATE DEHYDROGENASE).

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 most likely forms homotetramers.

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 D-3-PHOSPHOGLYCERATE DEHYDROGENASE (PHOSPHOGLYCERATE DEHYDROGENASE) P0A9T0 (2-410) (SERA_ECOLI)search Escherichia coli K-12search 99% 409 98%
B D-3-PHOSPHOGLYCERATE DEHYDROGENASE (PHOSPHOGLYCERATE DEHYDROGENASE) P0A9T0 (2-410) (SERA_ECOLI)search Escherichia coli K-12search 99% 409 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0A9T0 (2 - 410) D-3-PHOSPHOGLYCERATE DEHYDROGENASE (PHOSPHOGLYCERATE DEHYDROGENASE) Escherichia coli K-12

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P0A9T0) Formate/glycerate dehydrogenases, NAD-domainsearch, Formate/glycerate dehydrogenases, substrate-binding domainsearch, Phosphoglycerate dehydrogenase, regulatory (C-terminal) domainsearch NAD(P)-binding Rossmann-like Domainsearch, Alpha-Beta Plaitssearch PF00389: D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domainsearch, PF01842: ACT domainsearch, PF02826: D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P0A9T0) NAD bindingsearch oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptorsearch phosphoglycerate dehydrogenase activitysearch cofactor bindingsearch oxidoreductase activitysearch identical protein bindingsearch serine bindingsearch 2-hydroxyglutarate dehydrogenase activitysearch amino acid bindingsearch metabolic processsearch oxidation-reduction processsearch L-serine biosynthetic processsearch cellular amino acid biosynthetic processsearch

Chain InterPro annotation
A, B ACT domainsearch D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domainsearch D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domainsearch NAD(P)-binding domainsearch D-3-phosphoglycerate dehydrogenase, type2search D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain conserved site 1search D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain conserved sitesearch