MolNFT v1 · #85311 · protein
Protein crystallization and microgravity: glucose isomerase crystals grown during the pcdf-protein mission
4A8I · 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 0.73). MolNFT v1 #85311 on GenesisL1: 3D…
- PDB
- 4A8I
- 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 0.73
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
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.73 | 0.99 | 23 | empty |
| 2 | 462 | 0.65 | 0.77 | 47 | EDO |
| 3 | 65 | 0.43 | 0.81 | 14 | empty |
| 4 | 56 | 0.32 | 0.76 | 11 | empty |
| 5 | 68 | 0.29 | 0.73 | 15 | empty |
Compared structures
- 4A8I · 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 4A8I · PDBe 4A8I · UniProt P24300
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