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Crystal structure of human ribonucleotide reductase subunit R2

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

PDB: 2UW2
Type: protein
Length: 275 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonucleoside-diphosphate reductase M2 subunit
EC: 1.17.4.1
UniProt: P31350
Ligands: FE
Pockets: 3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonucleoside-diphosphate reductase M2 subunit (EC 1.17.4.1)	protein	275	69% helix, 0% strand	P31350

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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.55	0.88	17	empty
2	122	0.51	0.80	20	empty
3	53	0.28	0.74	14	empty

Compared structures

2UW2 · Crystal structure of human ribonucleotide reductase subunit R2 · the same entry in another collection · chain A against A, TM-score 1.00
P31350 · 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 P31350
Elsewhere: RCSB PDB 2UW2 · PDBe 2UW2 · UniProt P31350

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