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X-ray radiation dose series on xylose isomerase - 0.13 mgy

Analyse X-ray radiation dose series on xylose isomerase - 0.13 mgy in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6QRS
Type: protein
Length: 387 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, NA
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xylose isomerase (EC 5.3.1.5)	protein	387	50% helix, 11% strand	P24300

Ligands and binding sites

MN · Manganese (II) ion · metal · 2 copies · chains A
MG · Magnesium ion · metal · 2 copies · chains A
NA · Sodium ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 12 copies · chains A
IPA · Isopropyl alcohol · additive · 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	54	0.72	0.99	23	EDO
2	548	0.66	0.77	51	EDO
3	65	0.45	0.83	13	empty

Compared structures

6QRS · X-ray radiation dose series on xylose isomerase - 0.13 MGy · 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 6QRS · PDBe 6QRS · UniProt P24300

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