Research workbench
ALP1U_Y247F mutant in complex with fluostatin C
Analyse ALP1U_Y247F mutant in complex with fluostatin C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KXH
- Type
- protein
- Length
- 1,173 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative hydrolase
- EC
- 3.3.2.3
- UniProt
- Q1RQU8
- Ligands
- DY9, MLT, NA
- Pockets
- 12 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | Putative hydrolase (EC 3.3.2.3) | protein | 293 | 46% helix, 18% strand | Q1RQU8 |
| B | Putative hydrolase (EC 3.3.2.3) | protein | 294 | 45% helix, 19% strand | Q1RQU8 |
Ligands and binding sites
- DY9 · Fluostatin C · ligand · 4 copies · chains A, B, C, D
- MLT · D-malate · ligand · 2 copies · chains A, C, B, D
- NA · Sodium ion · metal · 3 copies · chains B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 846 | 0.76 | 0.80 | 110 | MLT |
| 2 | 382 | 0.73 | 0.84 | 39 | DY9 |
| 3 | 390 | 0.70 | 0.81 | 36 | DY9 |
| 4 | 385 | 0.70 | 0.81 | 33 | DY9 |
| 5 | 404 | 0.70 | 0.81 | 34 | DY9 |
Interfaces
5 interfaces between chains.
- A–D · 1645 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 1596 Ų buried · 16 hydrogen bonds · protein-protein
- B–D · 294 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 280 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 216 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6KXH · Alp1U_Y247F mutant in complex with Fluostatin C · 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 Q1RQU8
- Elsewhere: RCSB PDB 6KXH · PDBe 6KXH · UniProt Q1RQU8
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