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D71G/E101G/M234L mutant in organophosphorus hydrolase from deinococcus radiodurans

Analyse D71G/E101G/M234L mutant in organophosphorus hydrolase from deinococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GTI
Type: protein
Length: 331 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Organophosphorus hydrolase
UniProt: Q9RVU2
Ligands: NA, CO
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Organophosphorus hydrolase	protein	331	45% helix, 15% strand	Q9RVU2

Ligands and binding sites

NA · Sodium ion · metal · 3 copies · chains A
CO · Cobalt (II) ion · metal · 2 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	191	0.51	0.77	34	empty

Modifications

Observed in the structure: 1 modified (carboxylation).

Compared structures

3GTI · D71G/E101G/M234L mutant in organophosphorus hydrolase 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 Q9RVU2
Elsewhere: RCSB PDB 3GTI · PDBe 3GTI · UniProt Q9RVU2

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