MolNFT v1 · #175217 · protein

Crystal structure of metal-bound state of glucose isomerase

7CJO · Xylose isomerase: “Crystal structure of metal-bound state of glucose isomerase”. X-ray diffraction, 1 ligand (MG), 8 pockets (best druggability 0.76). MolNFT v1 #175217 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7CJO
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
Ligands: MG
Pockets: 8 · best druggability 0.76

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Xylose isomerase (EC 5.3.1.5)	protein	386	50% helix, 11% strand	P24300

Ligands and binding sites

MG · Magnesium ion · metal · 4 copies · chains A, B
EDO · 1,2-ethanediol · additive · 21 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	73	0.76	0.99	25	EDO
2	66	0.74	0.99	24	EDO
3	478	0.64	0.77	52	EDO
4	478	0.64	0.76	47	EDO
5	212	0.60	0.81	38	EDO

Interfaces

1 interface between chains.

A–B · 4847 Å² buried · 82 hydrogen bonds · protein-protein

Compared structures

7CJO · Crystal structure of metal-bound 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 7CJO · PDBe 7CJO · UniProt P24300

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