1nww Summary


Limonene-1,2-epoxide hydrolase

The structure was published by Arand, M., Hallberg, B.M., Zou, J., et al., de Bont, J.A.M., Jones, T.A., and Mowbray, S.L., in 2003 in a paper entitled "Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.2 Å and deposited in 2003.

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

This PDB entry contains multiple copies of the structure of Limonene-1,2-epoxide 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 homodimers.

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 Limonene-1,2-epoxide hydrolase Q9ZAG3 (1-149) (LIMA_RHOER)search Rhodococcus erythropolissearch 99% 149 97%
B Limonene-1,2-epoxide hydrolase Q9ZAG3 (1-149) (LIMA_RHOER)search Rhodococcus erythropolissearch 99% 149 97%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9ZAG3 (1 - 149) Limonene-1,2-epoxide hydrolase Rhodococcus erythropolis

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (Q9ZAG3) Limonene-1,2-epoxide hydrolase-likesearch Nuclear Transport Factor 2; Chain: A,search PF07858: Limonene-1,2-epoxide hydrolase catalytic domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (Q9ZAG3) limonene-1,2-epoxide hydrolase activitysearch hydrolase activitysearch metabolic processsearch

Chain InterPro annotation
A, B Limonene-1,2-epoxide hydrolasesearch