1WAE

Crystal structure of H129V Mutant of Alcaligenes Xylosoxidans Nitrite Reductase

Summary for 1WAE

Entry DOI	10.2210/pdb1wae/pdb
Related	1BQ5 1GS6 1GS7 1GS8 1HAU 1HAW 1NDT 1OE1 1OE2 1OE3 1WA0 1WA1 1WA2
Descriptor	DISSIMILATORY COPPER-CONTAINING NITRITE REDUCTASE, COPPER (II) ION, ZINC ION, ... (4 entities in total)
Functional Keywords	copper protein, oxidoreductase
Biological source	ALCALIGENES XYLOSOXYDANS
Total number of polymer chains	1
Total formula weight	36724.01
Authors	Ellis, M.J.,Antonyuk, S.V.,Strange, R.W.,Sawers, G.,Eady, R.R.,Hasnain, S.S. (deposition date: 2004-10-26, release date: 2004-10-28, Last modification date: 2023-12-13)
Primary citation	Ellis, M.J.,Antonyuk, S.V.,Strange, R.W.,Sawers, G.,Eady, R.R.,Hasnain, S.S. Observation of an Unprecedented Cu Bis-His Site: Crystal Structure of the H129V Mutant of Nitrite Reductase Inorg.Chem., 43:7591-, 2004 Cited by PubMed Abstract: Copper nitrite reductases contain both an electron-transfer type 1 Cu site and a catalytic type 2 Cu site. We have mutated one of the type 2 copper ligating histidines to observe the effect on catalytic turnover. This mutation has created a unique site where Cu is ligated by 2 His Nepsilon2 atoms alone. PubMed: 15554622 DOI: 10.1021/IC048966P PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.95 Å)

Structure validation