1b3r Summary



The structure was published by Hu, Y., Komoto, J., Huang, Y., et al., Takata, Y., Fujioka, M., and Takusagawa, F., in 1999 in a paper entitled "Crystal structure of S-adenosylhomocysteine hydrolase from rat liver." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 1998.

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

This PDB entry contains multiple copies of the structure of PROTEIN (S-ADENOSYLHOMOCYSTEINE HYDROLASE).

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 PROTEIN (S-ADENOSYLHOMOCYSTEINE HYDROLASE) P10760 (2-432) (SAHH_RAT)search Rattus norvegicussearch 100% 431 99%
B PROTEIN (S-ADENOSYLHOMOCYSTEINE HYDROLASE) P10760 (2-432) (SAHH_RAT)search Rattus norvegicussearch 100% 431 99%
C PROTEIN (S-ADENOSYLHOMOCYSTEINE HYDROLASE) P10760 (2-432) (SAHH_RAT)search Rattus norvegicussearch 100% 431 99%
D PROTEIN (S-ADENOSYLHOMOCYSTEINE HYDROLASE) P10760 (2-432) (SAHH_RAT)search Rattus norvegicussearch 100% 431 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P10760) Formate/glycerate dehydrogenases, NAD-domainsearch, S-adenosylhomocystein hydrolasesearch Rossmann foldsearch, NAD(P)-binding Rossmann-like Domainsearch PF00670: S-adenosyl-L-homocysteine hydrolase, NAD binding domainsearch, PF05221: S-adenosyl-L-homocysteine hydrolasesearch

Chain ID Cellular component (GO) Molecular function (GO) Biological process (GO)
A, B, C, D (P10760) nucleussearch extracellular vesicular exosomesearch neuron projectionsearch cytoplasmsearch cytosolsearch melanosomesearch adenyl nucleotide bindingsearch NAD bindingsearch hydrolase activitysearch adenosylhomocysteinase activitysearch identical protein bindingsearch circadian sleep/wake cyclesearch homocysteine biosynthetic processsearch S-adenosylmethionine cyclesearch response to hypoxiasearch one-carbon metabolic processsearch chronic inflammatory response to antigenic stimulussearch response to nutrientsearch S-adenosylhomocysteine catabolic processsearch

Chain InterPro annotation
A, B, C, D Adenosylhomocysteinasesearch S-adenosyl-L-homocysteine hydrolase, NAD binding domainsearch NAD(P)-binding domainsearch S-adenosyl-L-homocysteine hydrolase, conserved sitesearch