Research workbench

Ribonucleotide reductase R2 subunit from E. COLI

Analyse Ribonucleotide reductase R2 subunit from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1AV8
Type: protein
Length: 680 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonucleotide reductase R2
EC: 1.17.4.1
UniProt: P69924
Ligands: FEO
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 70% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribonucleotide reductase R2 (EC 1.17.4.1)	protein	340	70% helix, 4% strand	P69924

Ligands and binding sites

FEO · Mu-oxo-diiron · ligand · 2 copies · chains A, B

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	117	0.73	0.93	25	empty
2	59	0.29	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 3125 Å² buried · 51 hydrogen bonds · protein-protein

Compared structures

1AV8 · Ribonucleotide reductase R2 subunit from E. COLI · the same entry in another collection · chain A against A, TM-score 1.00
P69924 · AlphaFold monomer V2.0 prediction for ribonucleoside-diphosphate reductase 1 subunit beta… · a predicted model of the same protein · chain A against A, TM-score 1.00

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 P69924
Elsewhere: RCSB PDB 1AV8 · PDBe 1AV8 · UniProt P69924

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