Research workbench
Crystal structure of serine acetyltransferase from E.COLI at 2.2A
Analyse Crystal structure of serine acetyltransferase from E.COLI at 2.2A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T3D
- Type
- protein
- Length
- 786 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine acetyltransferase
- EC
- 2.3.1.30
- UniProt
- P0A9D4
- Ligands
- CYS
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Serine acetyltransferase (EC 2.3.1.30) | protein | 262 | 45% helix, 14% strand | P0A9D4 |
Ligands and binding sites
- CYS · Cysteine · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.77 | 0.91 | 54 | CYS |
| 2 | 209 | 0.76 | 0.91 | 57 | CYS |
| 3 | 208 | 0.75 | 0.90 | 58 | CYS |
| 4 | 774 | 0.73 | 0.78 | 69 | empty |
| 5 | 51 | 0.28 | 0.75 | 12 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1434 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 1424 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1422 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 27 modified (engineered).
Compared structures
- 1T3D · Crystal structure of Serine Acetyltransferase from E.coli at 2.2A · the same entry in another collection · chain B against B, TM-score 1.00
- P0A9D4 · AlphaFold monomer V2.0 prediction for serine acetyltransferase (P0A9D4) · 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 P0A9D4
- Elsewhere: RCSB PDB 1T3D · PDBe 1T3D · UniProt P0A9D4
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