MolNFT v1 · #93605 · protein
Crystal structure of serine acetyltransferase from vibrio cholerae O1 biovar el tor N16961
4H7O: “Crystal structure of serine acetyltransferase from vibrio cholerae O1 biovar el tor N16961”. X-ray diffraction, 3 ligands (CYS, ARG, NA), 4 pockets (best druggability 0.80). MolNFT v1 #93605 on GenesisL1: 3D structure, binding sites…
- PDB
- 4H7O
- Type
- protein
- Length
- 774 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine acetyltransferase
- EC
- 2.3.1.30
- UniProt
- Q9KNT2
- Ligands
- CYS, ARG, NA
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Serine acetyltransferase (EC 2.3.1.30) | protein | 258 | 43% helix, 16% strand | Q9KNT2 |
Ligands and binding sites
- CYS · Cysteine · ligand · 3 copies · chains A, C, B
- ARG · Arginine · ligand · 3 copies · chains A, C, B
- NA · Sodium ion · metal · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 861 | 0.80 | 0.83 | 61 | ARG |
| 2 | 235 | 0.77 | 0.90 | 55 | CYS |
| 3 | 208 | 0.74 | 0.90 | 51 | CYS |
| 4 | 199 | 0.74 | 0.90 | 49 | CYS |
Interfaces
3 interfaces between chains.
- B–C · 1535 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 1501 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1497 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 4H7O · Crystal structure of Serine acetyltransferase from Vibrio cholerae O1 biovar El Tor N16961 · the same entry in another collection · chain B against B, 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 Q9KNT2
- Elsewhere: RCSB PDB 4H7O · PDBe 4H7O · UniProt Q9KNT2
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