Research workbench

Ribonucleotide reductase Y122 2,3-F2Y variant

Analyse Ribonucleotide reductase Y122 2,3-F2Y variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CI1
Type: protein
Length: 349 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonucleoside-diphosphate reductase 1, beta subunit, ferritin-like protein
EC: 1.17.4.1
UniProt: A0A0E1LZC3
Ligands: FEO, SO4, CL
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonucleoside-diphosphate reductase 1, beta subunit, ferritin-like protein (EC 1.17.4.1)	protein	349	69% helix, 4% strand	A0A0E1LZC3

Ligands and binding sites

FEO · Mu-oxo-diiron · ligand · chains A
SO4 · Sulfate ion · ion · 4 copies · chains A
CL · Chloride ion · ion · 2 copies · 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	69	0.30	0.74	19	empty

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

5CI1 · Ribonucleotide reductase Y122 2,3-F2Y variant · the same entry in another collection · 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 A0A0E1LZC3
Elsewhere: RCSB PDB 5CI1 · PDBe 5CI1 · UniProt A0A0E1LZC3

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