MolNFT v1 · #24356 · protein

Organic hydroperoxide resistance protein from deinococcus radiodurans

1USP: “Organic hydroperoxide resistance protein from deinococcus radiodurans”. X-ray diffraction, 2 pockets (best druggability 0.67). MolNFT v1 #24356 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1USP
Type: protein
Length: 271 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Organic hydroperoxide resistance protein
UniProt: Q9RTA8
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Organic hydroperoxide resistance protein	protein	137	34% helix, 31% strand	Q9RTA8
B	Organic hydroperoxide resistance protein	protein	134	35% helix, 30% strand	Q9RTA8

Ligands and binding sites

GOL · Glycerol · additive · 5 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	312	0.67	0.82	38	empty
2	256	0.64	0.82	33	GOL

Interfaces

1 interface between chains.

A–B · 2815 Å² buried · 56 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

1USP · Organic Hydroperoxide Resistance Protein from Deinococcus radiodurans · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9RTA8
Elsewhere: RCSB PDB 1USP · PDBe 1USP · UniProt Q9RTA8

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