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Periplasmic heme-binding protein rhut from roseiflexus sp. rs-1 in two-heme bound form (holo-2)

Analyse Periplasmic heme-binding protein rhut from roseiflexus sp. rs-1 in two-heme… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5GJ3
Type
protein
Length
270 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Periplasmic binding protein
UniProt
A5UZ69
Ligands
HEM, ZN
Pockets
1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeriplasmic binding proteinprotein27047% helix, 19% strandA5UZ69

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A
  • ZN · Zinc ion · metal · 4 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13800.620.7736HEM, ZN

Compared structures

  • 5GJ3 · Periplasmic heme-binding protein RhuT from Roseiflexus sp. RS-1 in two-heme bound form… · the same entry in another collection · chain A against A, TM-score 1.00

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