MolNFT v1 · #85314 · protein

Protein crystallization and microgravity: glucose isomerase crystals grown during the pcdf-protein mission

4A8L · Xylose isomerase: “Protein crystallization and microgravity: glucose isomerase crystals grown during the pcdf-protein mission”. X-ray diffraction, 1 ligand (CO), 5 pockets (best druggability 0.72). MolNFT v1 #85314 on GenesisL1: 3D…

PDB: 4A8L
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: P24300
Ligands: CO
Pockets: 5 · 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	P24300

Ligands and binding sites

CO · Cobalt (II) ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · additive · chains A

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

Pockets

5 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	55	0.72	0.99	22	empty
2	464	0.65	0.78	47	EDO
3	64	0.43	0.82	14	empty
4	54	0.32	0.77	11	empty
5	66	0.28	0.72	15	empty

Compared structures

4A8L · Protein crystallization and microgravity: glucose isomerase crystals grown during the… · 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 4A8L · PDBe 4A8L · UniProt P24300

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