1wnw Summary

pdbe.org/1wnw
spacer

D136N mutant of Heme Oxygenase from Corynebacterium diphtheriae (HmuO)

The structure was published by Matsui, T., Furukawa, M., Unno, M., Tomita, T., and Ikeda-Saito, M., in 2005 in a paper entitled "Roles of Distal Asp in Heme Oxygenase from Corynebacterium diphtheriae, HmuO: A WATER-DRIVEN OXYGEN ACTIVATION MECHANISM" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 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 Heme oxygenase.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 Heme oxygenase P71119 (1-215) (HMUO_CORDI)search Corynebacterium diphtheriae NCTC 13129search 100% 215 97%
B Heme oxygenase P71119 (1-215) (HMUO_CORDI)search Corynebacterium diphtheriae NCTC 13129search 100% 215 97%
C Heme oxygenase P71119 (1-215) (HMUO_CORDI)search Corynebacterium diphtheriae NCTC 13129search 100% 215 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P71119 (1 - 215) Heme oxygenase Corynebacterium diphtheriae

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C (P71119) Eukaryotic type heme oxygenasesearch Heme Oxygenase; Chain Asearch PF01126: Heme oxygenasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B, C (P71119) oxidoreductase activitysearch heme oxygenase (decyclizing) activitysearch metal ion bindingsearch heme oxidationsearch oxidation-reduction processsearch

Chain InterPro annotation
A, B, C Haem oxygenasesearch Haem oxygenase-likesearch Haem oxygenase-like, multi-helicalsearch Haem oxygenase conserved sitesearch