1b3r Summary

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RAT LIVER S-ADENOSYLHOMOCYSTEIN HYDROLASE

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
P10760 (2 - 432) PROTEIN (S-ADENOSYLHOMOCYSTEINE HYDROLASE) Rattus norvegicus

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 response to hypoxiasearch circadian sleep/wake cyclesearch homocysteine biosynthetic processsearch adenosylhomocysteinase activitysearch identical protein bindingsearch hydrolase activitysearch NAD bindingsearch adenyl nucleotide bindingsearch cytoplasmsearch nucleussearch melanosomesearch cytosolsearch 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