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Structure of the reduced (feii) co-sensing protein from R. rubrum

Analyse Structure of the reduced (feii) co-sensing protein from R. rubrum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1FT9
Type
protein
Length
416 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Carbon monoxide oxidation system transcription regulator
UniProt
P72322
Ligands
HEM
Pockets
7 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACarbon monoxide oxidation system transcription regulatorprotein21038% helix, 24% strandP72322
BCarbon monoxide oxidation system transcription regulatorprotein20640% helix, 25% strandP72322

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11680.710.8929HEM
21450.620.8422HEM
31760.520.7823empty
41240.450.7821empty
5970.360.7418empty

Interfaces

1 interface between chains.

  • A–B · 1457 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 1FT9 · Structure of the reduced (feii) co-sensing protein from R. rubrum · the same entry in another collection · chain A against A, TM-score 1.00

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