Research workbench
Crystal structure of ribosomal-protein-alanine N-acetyltransferase from brucella melitensis biovar abortus 2308
Analyse Crystal structure of ribosomal-protein-alanine N-acetyltransferase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N1L
- Type
- protein
- Length
- 2,254 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GCN5-related N-acetyltransferase
- EC
- 2.3.1.-
- UniProt
- Q2YLP8
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 14 distinct chains · 36% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GCN5-related N-acetyltransferase (EC 2.3.1.-) | protein | 143 | 37% helix, 37% strand | Q2YLP8 |
| B, I | GCN5-related N-acetyltransferase (EC 2.3.1.-) | protein | 143 | 36% helix, 37% strand | Q2YLP8 |
| C | GCN5-related N-acetyltransferase (EC 2.3.1.-) | protein | 137 | 37% helix, 38% strand | Q2YLP8 |
| D | GCN5-related N-acetyltransferase (EC 2.3.1.-) | protein | 141 | 37% helix, 37% strand | Q2YLP8 |
| E | GCN5-related N-acetyltransferase (EC 2.3.1.-) | protein | 141 | 37% helix, 38% strand | Q2YLP8 |
| F | GCN5-related N-acetyltransferase (EC 2.3.1.-) | protein | 141 | 33% helix, 37% strand | Q2YLP8 |
| G | GCN5-related N-acetyltransferase (EC 2.3.1.-) | protein | 140 | 37% helix, 37% strand | Q2YLP8 |
| H | GCN5-related N-acetyltransferase (EC 2.3.1.-) | protein | 144 | 35% helix, 36% strand | Q2YLP8 |
| J | GCN5-related N-acetyltransferase (EC 2.3.1.-) | protein | 134 | 37% helix, 39% strand | Q2YLP8 |
| K, L | GCN5-related N-acetyltransferase (EC 2.3.1.-) | protein | 148 | 32% helix, 35% strand | Q2YLP8 |
| M | GCN5-related N-acetyltransferase (EC 2.3.1.-) | protein | 139 | 37% helix, 36% strand | Q2YLP8 |
| N | GCN5-related N-acetyltransferase (EC 2.3.1.-) | protein | 140 | 38% helix, 37% strand | Q2YLP8 |
| O | GCN5-related N-acetyltransferase (EC 2.3.1.-) | protein | 134 | 37% helix, 39% strand | Q2YLP8 |
| P | GCN5-related N-acetyltransferase (EC 2.3.1.-) | protein | 138 | 38% helix, 38% strand | Q2YLP8 |
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 453 | 0.81 | 0.89 | 36 | empty |
| 2 | 443 | 0.80 | 0.88 | 37 | empty |
| 3 | 612 | 0.78 | 0.84 | 70 | empty |
| 4 | 453 | 0.77 | 0.86 | 56 | empty |
| 5 | 237 | 0.77 | 0.91 | 37 | empty |
Interfaces
25 interfaces between chains.
- I–L · 2344 Ų buried · 33 hydrogen bonds · protein-protein
- H–K · 2313 Ų buried · 36 hydrogen bonds · protein-protein
- B–E · 2292 Ų buried · 32 hydrogen bonds · protein-protein
- A–D · 2282 Ų buried · 33 hydrogen bonds · protein-protein
- C–G · 2243 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 7N1L · Crystal Structure of Ribosomal-protein-alanine N-acetyltransferase from Brucella… · 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 Q2YLP8
- Elsewhere: RCSB PDB 7N1L · PDBe 7N1L · UniProt Q2YLP8
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