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Neutron structure of the cyclic glucose bound xylose isomerase E186Q mutant

Analyse Neutron structure of the cyclic glucose bound xylose isomerase E186Q mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LNC
Type: protein
Length: 385 residues
Chains: 1
Method: neutron diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylose isomerase
EC: 5.3.1.5
UniProt: P24300
Ligands: GLC, MN, MG
Pockets: 5 · best druggability 0.71

Structure

neutron 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

GLC · alpha-D-glucopyranose · sugar · chains A
MN · Manganese (II) ion · metal · 2 copies · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

5 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	51	0.71	0.98	24	empty
2	472	0.65	0.77	44	GLC
3	75	0.43	0.81	14	empty
4	64	0.35	0.77	13	empty
5	67	0.29	0.73	16	empty

Compared structures

4LNC · Neutron structure of the cyclic glucose bound Xylose Isomerase E186Q mutant · 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 4LNC · PDBe 4LNC · UniProt P24300

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