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Crystal structure of T2D three-domain heme-cu nitrite reductase from ralstonia pickettii

Analyse Crystal structure of T2D 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: 6FJA
Type: protein
Length: 455 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: HEM, CU
Pockets: 5 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nitrite reductase (EC 1.7.2.1)	protein	455	21% helix, 33% strand	I6NAW4

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
CU · Copper (II) ion · metal · 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	533	0.75	0.83	68	HEM
2	88	0.45	0.80	21	empty
3	155	0.45	0.75	29	empty
4	102	0.43	0.78	24	empty
5	55	0.34	0.78	12	empty

Modifications

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

Compared structures

6FJA · Crystal structure of T2D three-domain heme-Cu nitrite reductase from Ralstonia pickettii · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt I6NAW4
Elsewhere: RCSB PDB 6FJA · PDBe 6FJA · UniProt I6NAW4

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