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Solution structure of the H-nox protein from shewanella woodyi in the FE(II)CO ligation state

Analyse Solution structure of the H-nox protein from shewanella woodyi in the FE(II)CO… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6OCV
Type
protein
Length
190 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heme no binding domain protein
UniProt
B1KIH6
Ligands
HEM, CMO
Pockets
3 · best druggability 0.79

Structure

solution nmr · 1 distinct chain · 51% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHeme no binding domain proteinprotein19051% helix, 15% strandB1KIH6

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · chains A
  • CMO · Carbon monoxide · ion · chains A

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111940.790.8077CMO, HEM
21010.580.8622empty
31350.500.8022empty

Compared structures

  • 6OCV · Solution structure of the H-NOX protein from Shewanella woodyi in the Fe(II)CO ligation… · the same entry in another collection · chain A against A, TM-score 1.00

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