Research workbench
Crystal structure of acetyltransferase (gnat family) from enterococcus faecalis
Analyse Crystal structure of acetyltransferase (gnat family) from enterococcus faecalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I00
- Type
- protein
- Length
- 2,381 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyltransferase, gnat family
- EC
- 2.3.1.1
- UniProt
- Q831Y9
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 3 distinct chains · 33% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyltransferase, gnat family (EC 2.3.1.1) | protein | 397 | 34% helix, 32% strand | Q831Y9 |
| B, D, E | Acetyltransferase, gnat family (EC 2.3.1.1) | protein | 396 | 32% helix, 32% strand | Q831Y9 |
| C, F | Acetyltransferase, gnat family (EC 2.3.1.1) | protein | 398 | 33% helix, 33% strand | Q831Y9 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1062 | 0.83 | 0.84 | 104 | empty |
| 2 | 290 | 0.83 | 0.94 | 42 | empty |
| 3 | 284 | 0.82 | 0.94 | 36 | empty |
| 4 | 1126 | 0.82 | 0.83 | 100 | empty |
| 5 | 1155 | 0.81 | 0.82 | 101 | empty |
Interfaces
12 interfaces between chains.
- C–D · 1707 Ų buried · 29 hydrogen bonds · protein-protein
- E–F · 1698 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 1640 Ų buried · 21 hydrogen bonds · protein-protein
- B–D · 598 Ų buried · 12 hydrogen bonds · protein-protein
- A–F · 589 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2I00 · Crystal structure of acetyltransferase (GNAT family) from Enterococcus faecalis · 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 Q831Y9
- Elsewhere: RCSB PDB 2I00 · PDBe 2I00 · UniProt Q831Y9
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