MolNFT v1 · #15121 · protein

The 0.86 ångström structure of xylose isomerase

1MUW: “The 0.86 ångström structure of xylose isomerase”. X-ray diffraction, 3 ligands (MN, MG, OH), 3 pockets (best druggability 0.72). MolNFT v1 #15121 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1MUW
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: P15587
Ligands: MN, MG, OH
Pockets: 3 · best druggability 0.72

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	386	50% helix, 10% strand	P15587

Ligands and binding sites

MN · Manganese (II) ion · metal · 2 copies · chains A
MG · Magnesium ion · metal · 2 copies · chains A
OH · Hydroxide ion · ion · 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	50	0.72	0.99	21	empty
2	485	0.64	0.77	47	OH
3	74	0.46	0.82	13	empty

Compared structures

1MUW · The 0.86 Angstrom Structure of Xylose Isomerase · the same entry in another collection · chain A against A, TM-score 1.00
P15587 · AlphaFold monomer V2.0 prediction for xylose isomerase (P15587) · 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 P15587
Elsewhere: RCSB PDB 1MUW · PDBe 1MUW · UniProt P15587

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