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Crystal structure of glucose isomerase from non-merohedrally twinned crystals

Analyse Crystal structure of glucose isomerase from non-merohedrally twinned crystals in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6OQZ
Type: protein
Length: 386 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, MG
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xylose isomerase (EC 5.3.1.5)	protein	386	51% helix, 10% strand	P24300

Ligands and binding sites

MN · Manganese (II) ion · metal · 2 copies · chains A
MG · Magnesium ion · metal · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	50	0.72	0.99	23	empty
2	441	0.65	0.78	49	MPD
3	59	0.43	0.83	13	empty
4	71	0.30	0.73	21	empty

Compared structures

6OQZ · Crystal structure of Glucose Isomerase from Non-merohedrally twinned crystals · 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 6OQZ · PDBe 6OQZ · UniProt P24300

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