MolNFT v1 · #27389 · protein

Modes of binding substrates and their analogues to the enzyme D-xylose isomerase

1XIC: “Modes of binding substrates and their analogues to the enzyme D-xylose isomerase”. X-ray diffraction, 2 ligands (XLS, MN), 3 pockets (best druggability 0.71). MolNFT v1 #27389 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 1XIC
Type: protein
Length: 385 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-xylose isomerase
EC: 5.3.1.5
UniProt: P24300
Ligands: XLS, MN
Pockets: 3 · best druggability 0.71

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	D-xylose isomerase (EC 5.3.1.5)	protein	385	51% helix, 10% strand	P24300

Ligands and binding sites

XLS · D-xylose · ligand · chains A
MN · Manganese (II) ion · metal · 2 copies · chains A

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

Pockets

3 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	53	0.71	0.98	25	empty
2	467	0.65	0.78	47	XLS
3	90	0.47	0.81	14	empty

Compared structures

1XIC · Modes of binding substrates and their analogues to the enzyme D-xylose isomerase · 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 1XIC · PDBe 1XIC · UniProt P24300

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