MolNFT v1 · #21379 · protein
Structure of serine acetyltransferase from haemophilis influenzae rd
1S80: “Structure of serine acetyltransferase from haemophilis influenzae rd”. X-ray diffraction, 16 pockets (best druggability 0.88). MolNFT v1 #21379 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1S80
- Type
- protein
- Length
- 1,446 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine acetyltransferase
- EC
- 2.3.1.30
- UniProt
- P43886
- Pockets
- 16 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Serine acetyltransferase (EC 2.3.1.30) | protein | 241 | 46% helix, 16% strand | P43886 |
Pockets
16 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1017 | 0.88 | 0.89 | 139 | empty |
| 2 | 90 | 0.77 | 0.99 | 24 | empty |
| 3 | 457 | 0.77 | 0.85 | 67 | empty |
| 4 | 446 | 0.76 | 0.85 | 72 | empty |
| 5 | 91 | 0.75 | 0.98 | 25 | empty |
Interfaces
15 interfaces between chains.
- D–E · 1232 Ų buried · 16 hydrogen bonds · protein-protein
- E–F · 1209 Ų buried · 16 hydrogen bonds · protein-protein
- D–F · 1193 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 1167 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1166 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 1S80 · Structure of Serine Acetyltransferase from Haemophilis influenzae Rd · the same entry in another collection · chain F against F, TM-score 1.00
- P43886 · AlphaFold monomer V2.0 prediction for serine acetyltransferase (P43886) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P43886
- Elsewhere: RCSB PDB 1S80 · PDBe 1S80 · UniProt P43886
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