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Structures of yeast ribonucleotide reductase I

Analyse Structures of yeast ribonucleotide reductase I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CVS
Type: protein
Length: 657 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonucleoside-diphosphate reductase large chain 1
EC: 1.17.4.1
UniProt: P21524
Pockets: 6 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonucleoside-diphosphate reductase large chain 1 (EC 1.17.4.1)	protein	657	46% helix, 11% strand	P21524

Pockets

6 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	224	0.61	0.81	33	empty
2	389	0.61	0.77	48	empty
3	128	0.44	0.76	15	empty
4	80	0.36	0.76	22	empty
5	57	0.30	0.75	17	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2CVS · Structures of Yeast Ribonucleotide Reductase I · the same entry in another collection · chain A against A, TM-score 1.00
P21524 · AlphaFold monomer V2.0 prediction for ribonucleoside-diphosphate reductase large chain 1… · 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 P21524
Elsewhere: RCSB PDB 2CVS · PDBe 2CVS · UniProt P21524

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