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Crystal structure of metal-free state of glucose isomerase

Analyse Crystal structure of metal-free state of glucose isomerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CJP
Type: protein
Length: 772 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylose isomerase
EC: 5.3.1.5
UniProt: P24300
Pockets: 8 · best druggability 0.75

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Xylose isomerase (EC 5.3.1.5)	protein	386	49% helix, 11% strand	P24300

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 23 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	67	0.75	0.99	24	EDO
2	67	0.74	0.98	25	EDO
3	491	0.65	0.77	52	EDO
4	480	0.65	0.77	47	EDO
5	220	0.62	0.82	37	EDO

Interfaces

1 interface between chains.

A–B · 4862 Å² buried · 77 hydrogen bonds · protein-protein

Compared structures

7CJP · Crystal structure of metal-free state of glucose isomerase · 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 7CJP · PDBe 7CJP · UniProt P24300

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