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Protein R2 of ribonucleotide reductase from mouse

Analyse Protein R2 of ribonucleotide reductase from mouse in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XSM
Type: protein
Length: 288 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonucleotide reductase R2
EC: 1.17.4.1
UniProt: P11157
Ligands: FE
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonucleotide reductase R2 (EC 1.17.4.1)	protein	288	72% helix, 0% strand	P11157

Ligands and binding sites

FE · Fe (III) ion · metal · chains A

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

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	154	0.56	0.81	22	empty
2	117	0.43	0.77	20	empty

Compared structures

1XSM · Protein R2 of ribonucleotide reductase from mouse · the same entry in another collection · chain A against A, TM-score 1.00
P11157 · AlphaFold monomer V2.0 prediction for ribonucleoside-diphosphate reductase subunit M2… · 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 P11157
Elsewhere: RCSB PDB 1XSM · PDBe 1XSM · UniProt P11157

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