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Structure and function of the escherichia COLI ribonucleotide reductase protein R2

Analyse Structure and function of the escherichia COLI ribonucleotide reductase protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RIB
Type: protein
Length: 680 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonucleotide reductase R1 protein
EC: 1.17.4.1
UniProt: P69924
Ligands: FEO
Pockets: 3 · best druggability 0.74

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribonucleotide reductase R1 protein (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

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	128	0.74	0.93	27	empty
2	69	0.52	0.86	18	empty
3	50	0.26	0.74	11	empty

Interfaces

1 interface between chains.

A–B · 3081 Å² buried · 46 hydrogen bonds · protein-protein

Compared structures

1RIB · Structure and function of the escherichia COLI ribonucleotide reductase protein R2 · the same entry in another collection · chain A against A, TM-score 1.00

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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 1RIB · PDBe 1RIB · UniProt P69924

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