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Crystal structure of glucose isomerase by fixed-target serial synchrotron crystallography (500 ms)

Analyse Crystal structure of glucose isomerase by fixed-target serial synchrotron… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CVM
Type: protein
Length: 385 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: MG
Pockets: 4 · best druggability 0.74

Structure

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

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

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A

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

Pockets

4 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	60	0.74	0.99	24	empty
2	494	0.66	0.78	45	empty
3	78	0.48	0.83	15	empty
4	52	0.32	0.77	13	empty

Compared structures

7CVM · Crystal structure of glucose isomerase by fixed-target serial synchrotron crystallography… · 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 7CVM · PDBe 7CVM · UniProt P24300

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