MolNFT v1 · #66026 · protein

Structural study of clostridium thermocellum ribose-5-phosphate isomerase B

3HE8: “Structural study of clostridium thermocellum ribose-5-phosphate isomerase B”. X-ray diffraction, 3 pockets (best druggability 0.56). MolNFT v1 #66026 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3HE8
Type: protein
Length: 296 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribose-5-phosphate isomerase
EC: 5.3.1.6
UniProt: A3DIL8
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribose-5-phosphate isomerase (EC 5.3.1.6)	protein	148	51% helix, 16% strand	A3DIL8

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

3 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	57	0.56	0.90	17	GOL
2	52	0.56	0.90	15	empty
3	53	0.54	0.90	17	GOL

Interfaces

1 interface between chains.

A–B · 2049 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

3HE8 · Structural study of Clostridium thermocellum Ribose-5-Phosphate Isomerase B · 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 A3DIL8
Elsewhere: RCSB PDB 3HE8 · PDBe 3HE8 · UniProt A3DIL8

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