GL1X · GenesisL1 explorer

Research workbench

Ohra (organic hydroperoxide resistance protein) mutant (C61S) in the "open conformation" from chromobacterium violaceum

Analyse Ohra (organic hydroperoxide resistance protein) mutant (C61S) in the "open… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ED0
Type
protein
Length
292 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Organic hydroperoxide resistance protein
UniProt
Q7P1K4
Ligands
SO4
Pockets
2 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOrganic hydroperoxide resistance proteinprotein15031% helix, 29% strandQ7P1K4
BOrganic hydroperoxide resistance proteinprotein14233% helix, 30% strandQ7P1K4

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11370.450.7719empty
21070.440.7820empty

Interfaces

1 interface between chains.

  • A–B · 3901 Ų buried · 69 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

  • 6ED0 · OhrA (Organic Hydroperoxide Resistance protein) mutant (C61S) in the "open conformation"… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.