MolNFT v1 · #162922 · protein
Liquid application method for time-resolved analyses (lama) by serial synchrotron crystallography, xylose isomerase 15 ms timepoint
6RND: “Liquid application method for time-resolved analyses (lama) by serial synchrotron crystallography, xylose…”. X-ray diffraction, 2 ligands (GLC, MG), 4 pockets (best druggability 0.73). MolNFT v1 #162922 on GenesisL1: 3D structure…
- PDB
- 6RND
- Type
- protein
- Length
- 387 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
- GLC, MG
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xylose isomerase (EC 5.3.1.5) | protein | 387 | 50% helix, 11% strand | P24300 |
Ligands and binding sites
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.73 | 0.99 | 24 | empty |
| 2 | 534 | 0.67 | 0.77 | 56 | GLC |
| 3 | 74 | 0.44 | 0.81 | 14 | empty |
| 4 | 59 | 0.28 | 0.73 | 15 | empty |
Compared structures
- 6RND · Liquid Application Method for time-resolved Analyses (LAMA) by serial synchrotron… · 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 6RND · PDBe 6RND · UniProt P24300
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