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PDB entry 1u8f

Crystal Structure Of Human Placental Glyceraldehyde-3-Phosphate Dehydrogenase At 1.75 Resolution

The structure was published by Jenkins, J.L. and Tanner, J.J., in 2006 in a paper entitled "High-resolution structure of human D-glyceraldehyde-3-phosphate dehydrogenase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.75 Å and deposited in 2004.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Glyceraldehyde-3-phosphate dehydrogenase, liver.

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
O Glyceraldehyde-3-phosphate dehydrogenase, liver P04406 (1-335) (G3P_HUMAN)search Homo sapienssearch 100% 335 99%
P Glyceraldehyde-3-phosphate dehydrogenase, liver P04406 (1-335) (G3P_HUMAN)search Homo sapienssearch 100% 335 99%
Q Glyceraldehyde-3-phosphate dehydrogenase, liver P04406 (1-335) (G3P_HUMAN)search Homo sapienssearch 100% 335 99%
R Glyceraldehyde-3-phosphate dehydrogenase, liver P04406 (1-335) (G3P_HUMAN)search Homo sapienssearch 100% 335 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04406 (1 - 335) Glyceraldehyde-3-phosphate dehydrogenase, liver Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
O, P, Q, R (P04406) Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domainsearch, GAPDH-likesearch NAD(P)-binding Rossmann-like Domainsearch, Dihydrodipicolinate Reductase; domain 2search Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domainsearch, Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domainsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
O, P, Q, R (P04406) Nucleotide bindingsearch, Glyceraldehyde-3-phosphate dehydrogenase (nad+) (phosphorylating) activitysearch, Protein bindingsearch, Oxidoreductase activitysearch, Oxidoreductase activity, acting on the aldehyde or oxo group of donors, nad or nadp as acceptorsearch, Transferase activitysearch, Peptidyl-cysteine s-nitrosylase activitysearch, Nadp bindingsearch, Nad bindingsearch Nucleussearch, Cytoplasmsearch, Cytosolsearch, Membranesearch, Perinuclear region of cytoplasmsearch Carbohydrate metabolic processsearch, Glucose metabolic processsearch, Gluconeogenesissearch, Glycolysissearch, Apoptotic processsearch, Peptidyl-cysteine s-trans-nitrosylationsearch, Small molecule metabolic processsearch, Protein stabilizationsearch, Neuron apoptosissearch, Oxidation-reduction processsearch

Chain InterPro annotation
O, P, Q, R Glyceraldehyde-3-phosphate dehydrogenase, type Isearch, NAD(P)-binding domainsearch, Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domainsearch, Glyceraldehyde 3-phosphate dehydrogenase, catalytic domainsearch, Glyceraldehyde 3-phosphate dehydrogenase, active sitesearch, Glyceraldehyde/Erythrose phosphate dehydrogenase familysearch