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Crystal structure of the sixteen heme cytochrome from desulfovibrio gigas

Analyse Crystal structure of the sixteen heme cytochrome from desulfovibrio gigas in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Z1N
Type
protein
Length
516 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sixteen heme cytochrome
UniProt
Q8VUI3
Ligands
HEC, NAG, NAA, ZN
Pockets
8 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
XSixteen heme cytochromeprotein51639% helix, 8% strandQ8VUI3

Ligands and binding sites

  • HEC · Heme C · ligand · 16 copies · chains X
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains X
  • NAA · 2-acetamido-2-deoxy-beta-D-allopyranose · sugar
  • ZN · Zinc ion · metal · 3 copies · chains X
  • GOL · Glycerol · additive · 5 copies · chains X

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16480.820.8677ZN, HEC
22640.770.9048HEC
32320.750.8945HEC, GOL
41500.700.8932HEC
51300.690.9028HEC

Modifications

Observed in the structure: 30 cofactor, 1 glycan (heme c attachment, N-glycosylation).

Compared structures

  • 1Z1N · Crystal Structure of the sixteen heme cytochrome from Desulfovibrio gigas · the same entry in another collection · chain X against X, TM-score 1.00

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