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X-ray crystal structure of bacillus subtilis ribonucleotide reductase nrde alpha subunit (nucleotide free)

Analyse X-ray crystal structure of bacillus subtilis ribonucleotide reductase nrde… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6CGM
Type: protein
Length: 657 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonucleoside-diphosphate reductase
EC: 1.17.4.1
UniProt: A0A162Q3J9
Pockets: 9 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonucleoside-diphosphate reductase (EC 1.17.4.1)	protein	657	48% helix, 13% strand	A0A162Q3J9

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	420	0.66	0.79	58	empty
2	63	0.51	0.86	16	empty
3	205	0.50	0.76	29	EDO
4	132	0.48	0.79	27	empty
5	84	0.35	0.75	17	empty

Compared structures

6CGM · X-ray crystal structure of Bacillus subtilis ribonucleotide reductase NrdE alpha subunit… · 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 A0A162Q3J9
Elsewhere: RCSB PDB 6CGM · PDBe 6CGM · UniProt A0A162Q3J9

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