Hydroxylamine oxidoreductase from nitrosomonas europaea

Structure

x-ray diffraction · 2 distinct chains · 53% helix, 5% strand (DSSP).

Ligands and binding sites

• HEC · Heme C · ligand · 42 copies · chains A, C, E, G, I, K
• ISW · {3,3'-[(9S)-8,13-diethenyl-3,7,12,17-tetramethyl-9,10-dihydroporphyrin-2,18-diyl-kappa~4~n~21~,n~22~,n~23~, n~24~]dipropanoato(2-)}iron · ligand · 6 copies · chains A, C, E, G, I, K
• PGE · Triethylene glycol · additive · 8 copies · chains A, C, E, G, I
• PEG · Di(hydroxyethyl)ether · additive · 6 copies · chains A, C, G, J, K
• PG4 · Tetraethylene glycol · additive · 4 copies · chains A, C, E, K

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Interfaces

21 interfaces between chains.

• G–I · 2844 Ų buried · 43 hydrogen bonds · protein-protein
• A–E · 2844 Ų buried · 44 hydrogen bonds · protein-protein
• G–K · 2798 Ų buried · 37 hydrogen bonds · protein-protein
• C–E · 2797 Ų buried · 37 hydrogen bonds · protein-protein
• A–C · 2795 Ų buried · 39 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 84 cofactor, 18 covalent, 6 disulfide (heme c attachment, covalent ligand, disulfide).

Compared structures

• 6M0Q · Hydroxylamine oxidoreductase from Nitrosomonas europaea · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt A0A1I0F3S0
• Every structure of UniProt A0A1H9ZKV8
• Elsewhere: RCSB PDB 6M0Q · PDBe 6M0Q · UniProt A0A1I0F3S0 · UniProt A0A1H9ZKV8