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Structure of ribonucleotide reductase from rhodobacter sphaeroides

Analyse Structure of ribonucleotide reductase from rhodobacter sphaeroides in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7B9P
Type: protein
Length: 899 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vitamin B12-dependent ribonucleotide reductase
EC: 1.17.4.1
UniProt: Q3J3H6
Ligands: DTP, MG
Pockets: 7 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vitamin B12-dependent ribonucleotide reductase (EC 1.17.4.1)	protein	899	42% helix, 13% strand	Q3J3H6

Ligands and binding sites

DTP · 2'-deoxyadenosine 5'-triphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

7 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	930	0.75	0.78	96	empty
2	216	0.63	0.82	29	empty
3	261	0.56	0.77	31	empty
4	113	0.36	0.74	22	empty
5	67	0.30	0.74	14	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7B9P · Structure of Ribonucleotide reductase from Rhodobacter sphaeroides · 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 Q3J3H6
Elsewhere: RCSB PDB 7B9P · PDBe 7B9P · UniProt Q3J3H6

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