MolNFT v1 · #161962 · protein

Protein crystallization by ionic liquid hydrogel support: reference crystal of glucose isomerase grown on standard silanized glass

6QUF · Xylose isomerase: “Protein crystallization by ionic liquid hydrogel support: reference crystal of glucose isomerase grown on…”. X-ray diffraction, 2 ligands (MN, SO4), 2 pockets (best druggability 0.65). MolNFT v1 #161962 on…

PDB: 6QUF
Type: protein
Length: 385 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylose isomerase
EC: 5.3.1.5
UniProt: P24300
Ligands: MN, SO4
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xylose isomerase (EC 5.3.1.5)	protein	385	50% helix, 10% strand	P24300

Ligands and binding sites

MN · Manganese (II) ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 3 copies · chains A

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	457	0.65	0.78	45	GOL
2	67	0.45	0.83	13	empty

Compared structures

6QUF · Protein crystallization by ionic liquid hydrogel support: reference crystal of glucose… · 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 P24300
Elsewhere: RCSB PDB 6QUF · PDBe 6QUF · UniProt P24300

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