Research workbench
Crystal structure of neisseria gonorrhoeae serine acetyltransferase (cyse)
Analyse Crystal structure of neisseria gonorrhoeae serine acetyltransferase (cyse) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WYE
- Type
- protein
- Length
- 1,534 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine acetyltransferase
- EC
- 2.3.1.30
- UniProt
- A0A1D3FX11
- Ligands
- LMR, NA
- Pockets
- 18 · best druggability 0.79
Structure
x-ray diffraction · 6 distinct chains · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine acetyltransferase (EC 2.3.1.30) | protein | 261 | 43% helix, 15% strand | A0A1D3FX11 |
| B | Serine acetyltransferase (EC 2.3.1.30) | protein | 255 | 42% helix, 16% strand | A0A1D3FX11 |
| C | Serine acetyltransferase (EC 2.3.1.30) | protein | 254 | 43% helix, 14% strand | A0A1D3FX11 |
| D | Serine acetyltransferase (EC 2.3.1.30) | protein | 250 | 43% helix, 14% strand | A0A1D3FX11 |
| E | Serine acetyltransferase (EC 2.3.1.30) | protein | 256 | 43% helix, 16% strand | A0A1D3FX11 |
| F | Serine acetyltransferase (EC 2.3.1.30) | protein | 258 | 43% helix, 16% strand | A0A1D3FX11 |
Ligands and binding sites
- LMR · (2S)-2-hydroxybutanedioic acid · ligand · 6 copies · chains A, C, B, D, F, E
- NA · Sodium ion · metal · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 134 | 0.79 | 0.97 | 42 | LMR |
| 2 | 633 | 0.72 | 0.79 | 52 | empty |
| 3 | 315 | 0.71 | 0.84 | 54 | LMR |
| 4 | 353 | 0.71 | 0.83 | 60 | LMR |
| 5 | 337 | 0.68 | 0.82 | 58 | LMR |
Interfaces
6 interfaces between chains.
- D–F · 1419 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 1234 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 1222 Ų buried · 11 hydrogen bonds · protein-protein
- B–F · 1164 Ų buried · 11 hydrogen bonds · protein-protein
- D–E · 297 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6WYE · Crystal structure of Neisseria gonorrhoeae serine acetyltransferase (CysE) · 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 A0A1D3FX11
- Elsewhere: RCSB PDB 6WYE · PDBe 6WYE · UniProt A0A1D3FX11
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