Research workbench
Crystal structure of N-acetyltransferase from staphylococcus aureus MU50
Analyse Crystal structure of N-acetyltransferase from staphylococcus aureus MU50 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M85
- Type
- protein
- Length
- 735 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyltransferase
- UniProt
- Q99V53
- Pockets
- 7 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 43% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetyltransferase | protein | 185 | 42% helix, 26% strand | Q99V53 |
| B | N-acetyltransferase | protein | 184 | 43% helix, 28% strand | Q99V53 |
| C, D | N-acetyltransferase | protein | 183 | 44% helix, 26% strand | Q99V53 |
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 967 | 0.74 | 0.77 | 79 | empty |
| 2 | 430 | 0.69 | 0.80 | 39 | empty |
| 3 | 279 | 0.65 | 0.81 | 30 | empty |
| 4 | 339 | 0.64 | 0.79 | 35 | empty |
| 5 | 280 | 0.57 | 0.77 | 40 | empty |
Interfaces
5 interfaces between chains.
- B–C · 850 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 500 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 131 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 75 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 35 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4M85 · Crystal structure of N-acetyltransferase from Staphylococcus aureus Mu50 · 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 Q99V53
- Elsewhere: RCSB PDB 4M85 · PDBe 4M85 · UniProt Q99V53
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