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Crystal structure of deinococcus radiodurans ro (rsr) protein

Analyse Crystal structure of deinococcus radiodurans ro (rsr) protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NVO
Type: protein
Length: 496 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ro sixty-related protein, rsr
UniProt: Q9RUW8
Ligands: CA
Pockets: 7 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ro sixty-related protein, rsr	protein	496	54% helix, 9% strand	Q9RUW8

Ligands and binding sites

CA · Calcium ion · metal · chains A

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	69	0.73	0.97	20	empty
2	54	0.53	0.88	13	empty
3	61	0.51	0.86	18	empty
4	124	0.42	0.76	24	empty
5	132	0.41	0.75	23	empty

Compared structures

2NVO · Crystal structure of Deinococcus radiodurans RO (RSR) protein · the same entry in another collection · chain A against A, TM-score 1.00
Q9RUW8 · AlphaFold monomer V2.0 prediction for 60 kda ss-A/RO ribonucleoprotein homolog (Q9RUW8) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9RUW8
Elsewhere: RCSB PDB 2NVO · PDBe 2NVO · UniProt Q9RUW8

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