4O65: Crystal Structure Of The Cupredoxin Domain Of Amob From Nitrosocaldus Yellowstonii

The ammonia monooxygenase (AMO)/particulate methane monooxygenase (pMMO) superfamily is a diverse group of membrane-bound enzymes of which only pMMO has been characterized on the molecular level. The pMMO active site is believed to reside in the soluble N-terminal region of the pmoB subunit. To understand the degree of structural conservation within this superfamily, the crystal structure of the corresponding domain of an archaeal amoB subunit from Nitrosocaldus yellowstonii has been determined to 1.8 A resolution. The structure reveals a remarkable conservation of overall fold and copper binding site location as well as several notable differences that may have implications for function and stability. Proteins 2014; 82:2263-2267. (c) 2014 Wiley Periodicals, Inc.
PDB ID: 4O65Download
MMDB ID: 118870
PDB Deposition Date: 2013/12/20
Updated in MMDB: 2014/09
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 4O65: monomeric; determined by author and by software (PISA)
Molecular Components in 4O65
Label Count Molecule
Protein (1 molecule)
Putative Archaeal Ammonia Monooxygenase Subunit B
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

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