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Crystal structure of DR0079 from deinococcus radiodurans at 1.9 ångström resolution

Analyse Crystal structure of DR0079 from deinococcus radiodurans at 1.9 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O5F
Type: protein
Length: 317 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative nudix hydrolase DR_0079
EC: 3.6.-.-
UniProt: Q9RY71
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative nudix hydrolase DR_0079 (EC 3.6.-.-)	protein	155	24% helix, 34% strand	Q9RY71
B	Putative nudix hydrolase DR_0079 (EC 3.6.-.-)	protein	162	23% helix, 34% strand	Q9RY71

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	279	0.61	0.80	38	empty
2	135	0.43	0.76	26	empty

Interfaces

1 interface between chains.

A–B · 539 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2O5F · Crystal Structure of DR0079 from Deinococcus radiodurans at 1.9 Angstrom Resolution · the same entry in another collection · chain A against A, TM-score 1.00
Q9RY71 · AlphaFold monomer V2.0 prediction for nudix hydrolase DR_0079 (Q9RY71) · a predicted model of the same protein · chain B against A, TM-score 0.99

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9RY71
Elsewhere: RCSB PDB 2O5F · PDBe 2O5F · UniProt Q9RY71

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