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Joint neutron and X-ray structure of apo-D-xylose isomerase at PH=5.9

Analyse Joint neutron and X-ray structure of apo-D-xylose isomerase at PH=5.9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3QZA
Type: protein
Length: 388 residues
Chains: 1
Method: neutron diffraction; x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylose isomerase
EC: 5.3.1.5
UniProt: P24300
Pockets: 2 · best druggability 0.65

Structure

neutron diffraction; x-ray diffraction · 1 distinct chain · 49% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xylose isomerase (EC 5.3.1.5)	protein	388	49% helix, 11% strand	P24300

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	448	0.65	0.77	44	empty
2	83	0.47	0.82	13	empty

Compared structures

3QZA · Joint neutron and X-ray structure of apo-D-Xylose Isomerase at pH=5.9 · the same entry in another collection · chain A against A, TM-score 1.00
P24300 · AlphaFold monomer V2.0 prediction for xylose isomerase (P24300) · a predicted model of the same protein · 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 3QZA · PDBe 3QZA · UniProt P24300

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