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Crystal structure of ribose-5-phosphate isomerase a from burkholderia thailandensis

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

PDB: 3U7J
Type: protein
Length: 231 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribose-5-phosphate isomerase a
EC: 5.3.1.6
UniProt: Q2SVL4
Ligands: K, SO4
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribose-5-phosphate isomerase a (EC 5.3.1.6)	protein	231	35% helix, 29% strand	Q2SVL4

Ligands and binding sites

K · Potassium ion · metal · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 5 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	60	0.35	0.79	18	SO4, EDO, K

Compared structures

3U7J · Crystal structure of Ribose-5-phosphate isomerase A from Burkholderia thailandensis · 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 Q2SVL4
Elsewhere: RCSB PDB 3U7J · PDBe 3U7J · UniProt Q2SVL4

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