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Crystal structure of three-domain heme-cu nitrite reductase from ralstonia pickettii in I213 space group

Analyse Crystal structure of three-domain heme-cu nitrite reductase from ralstonia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6F1Q
Type: protein
Length: 456 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nitrite reductase
EC: 1.7.2.1
UniProt: I6NAW4
Ligands: HEC, CU
Pockets: 5 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nitrite reductase (EC 1.7.2.1)	protein	456	20% helix, 33% strand	I6NAW4

Ligands and binding sites

HEC · Heme C · ligand · chains A
CU · Copper (II) ion · metal · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	540	0.77	0.84	68	HEC
2	142	0.46	0.77	29	empty
3	70	0.43	0.81	20	empty
4	80	0.38	0.77	17	empty
5	51	0.28	0.75	20	empty

Modifications

Observed in the structure: 2 cofactor (heme c attachment).

Compared structures

6F1Q · Crystal structure of three-domain heme-Cu nitrite reductase from Ralstonia pickettii in… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt I6NAW4
Elsewhere: RCSB PDB 6F1Q · PDBe 6F1Q · UniProt I6NAW4

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