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Crystal structure of thermus thermophilus ribose-5-phosphate isomerase

Analyse Crystal structure of thermus thermophilus ribose-5-phosphate isomerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UJ4
Type: protein
Length: 225 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribose 5-phosphate isomerase
EC: 5.3.1.6
UniProt: Q72J47
Ligands: CL
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribose 5-phosphate isomerase (EC 5.3.1.6)	protein	225	31% helix, 29% strand	Q72J47

Ligands and binding sites

CL · Chloride ion · ion · 3 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	115	0.44	0.78	27	CL

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

1UJ4 · Crystal structure of Thermus thermophilus ribose-5-phosphate isomerase · the same entry in another collection · chain A against A, TM-score 1.00
Q72J47 · AlphaFold monomer V2.0 prediction for ribose-5-phosphate isomerase a (Q72J47) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q72J47
Elsewhere: RCSB PDB 1UJ4 · PDBe 1UJ4 · UniProt Q72J47

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