MolNFT v1 · #61316 · protein

Apo (iron free) structure of C. ammoniagenes R2 protein

3DHZ · Ribonucleotide reductase subunit R2F: “Apo (iron free) structure of C. ammoniagenes R2 protein”. X-ray diffraction, 1 ligand (FE2), 2 pockets (best druggability 0.57). MolNFT v1 #61316 on GenesisL1: 3D structure, binding sites and…

PDB: 3DHZ
Type: protein
Length: 591 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonucleotide reductase subunit R2F
UniProt: O69274
Ligands: FE2
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonucleotide reductase subunit R2F	protein	295	78% helix, 0% strand	O69274
B	Ribonucleotide reductase subunit R2F	protein	296	77% helix, 0% strand	O69274

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

2 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	371	0.57	0.75	51	empty
2	55	0.28	0.74	13	empty

Interfaces

1 interface between chains.

A–B · 2740 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

3DHZ · Apo (iron free) structure of C. ammoniagenes R2 protein · 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 O69274
Elsewhere: RCSB PDB 3DHZ · PDBe 3DHZ · UniProt O69274

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