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Cytochrome C nitrite reductase

Analyse Cytochrome C nitrite reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1QDB
Type
protein
Length
1,419 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome C nitrite reductase
UniProt
Q9Z4P4
Ligands
HEC, CA, SO4
Pockets
13 · best druggability 0.89

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CCytochrome C nitrite reductaseprotein47353% helix, 8% strandQ9Z4P4

Ligands and binding sites

  • HEC · Heme C · ligand · 15 copies · chains A, B, C
  • CA · Calcium ion · metal · 3 copies · chains A, B, C
  • SO4 · Sulfate ion · ion · 9 copies · chains A, B, C

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

Pockets

13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19830.890.91128SO4, HEC
28590.890.92110SO4, HEC
311390.870.88115SO4, HEC
41460.720.9128empty
51650.690.8831empty

Interfaces

2 interfaces between chains.

  • A–B · 1764 Ų buried · 25 hydrogen bonds · protein-protein
  • B–C · 504 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 30 cofactor (heme c attachment).

Compared structures

  • 1QDB · Cytochrome C nitrite reductase · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9Z4P4 · AlphaFold monomer V2.0 prediction for cytochrome C-552 (Q9Z4P4) · a predicted model of the same protein · chain A against A, TM-score 1.00

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