MolNFT v1 · #25806 · protein

Crystal structure of mouse ribonucleotide reductase subunit R2 under oxidizing conditions. a fully occupied dinuclear iron cluster.

1W68 · Ribonucleoside-diphosphate reductase M2 chain: “Crystal structure of mouse ribonucleotide reductase subunit R2 under oxidizing conditions. a fully occupied…”. X-ray diffraction, 1 ligand (FEO), 1 pocket (best druggability 0.48).…

PDB: 1W68
Type: protein
Length: 281 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonucleoside-diphosphate reductase M2 chain
EC: 1.17.4.1
UniProt: P11157
Ligands: FEO
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonucleoside-diphosphate reductase M2 chain (EC 1.17.4.1)	protein	281	76% helix, 0% strand	P11157

Ligands and binding sites

FEO · Mu-oxo-diiron · ligand · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	148	0.48	0.77	20	empty

Compared structures

1W68 · Crystal Structure of Mouse Ribonucleotide Reductase Subunit R2 under Oxidizing… · 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 1W68 · PDBe 1W68 · UniProt P11157

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