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

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