Research workbench

Ribonucleotide reductase protein R1E from salmonella typhimurium

Analyse Ribonucleotide reductase protein R1E from salmonella typhimurium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PEM
Type: protein
Length: 682 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonucleoside-diphosphate reductase 2 alpha chain
EC: 1.17.4.1
UniProt: Q08698
Pockets: 11 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonucleoside-diphosphate reductase 2 alpha chain (EC 1.17.4.1)	protein	682	47% helix, 12% strand	Q08698

Pockets

11 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	512	0.68	0.78	71	empty
2	139	0.45	0.77	21	empty
3	56	0.42	0.82	17	empty
4	92	0.41	0.78	29	empty
5	101	0.41	0.76	14	empty

Compared structures

1PEM · Ribonucleotide Reductase Protein R1E from Salmonella typhimurium · the same entry in another collection · chain A against A, TM-score 1.00
Q08698 · AlphaFold monomer V2.0 prediction for ribonucleoside-diphosphate reductase 2 subunit… · 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 Q08698
Elsewhere: RCSB PDB 1PEM · PDBe 1PEM · UniProt Q08698

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