MolNFT v1 · #86973 · protein

Crystal structure of ribonucleotide reductase di-iron nrdf from bacillus cereus

4BMT · Ribonucleoside-diphosphate reductase subunit beta: “Crystal structure of ribonucleotide reductase di-iron nrdf from bacillus cereus”. X-ray diffraction, 1 ligand (FE2), 7 pockets (best druggability 0.51). MolNFT v1 #86973 on…

PDB: 4BMT
Type: protein
Length: 574 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonucleoside-diphosphate reductase subunit beta
EC: 1.17.4.1
UniProt: Q81G55
Ligands: FE2
Pockets: 7 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribonucleoside-diphosphate reductase subunit beta (EC 1.17.4.1)	protein	287	78% helix, 0% strand	Q81G55

Ligands and binding sites

FE2 · Fe (II) ion · metal · 4 copies · chains A, B

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

Pockets

7 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	184	0.51	0.77	28	empty
2	124	0.43	0.76	19	empty
3	95	0.41	0.77	14	empty
4	65	0.39	0.79	20	empty
5	57	0.39	0.80	17	empty

Interfaces

1 interface between chains.

A–B · 2283 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

4BMT · Crystal Structure of Ribonucleotide Reductase di-iron NrdF from Bacillus cereus · 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 Q81G55
Elsewhere: RCSB PDB 4BMT · PDBe 4BMT · UniProt Q81G55

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.