Research workbench
Crystal structure analysis of nocardia farcinica arylamine N- acetyltransferase
Analyse Crystal structure analysis of nocardia farcinica arylamine N- acetyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D9W
- Type
- protein
- Length
- 1,128 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative acetyltransferase
- EC
- 2.3.1.5
- UniProt
- Q5YYQ3
- Pockets
- 10 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative acetyltransferase (EC 2.3.1.5) | protein | 284 | 32% helix, 28% strand | Q5YYQ3 |
| B, D | Putative acetyltransferase (EC 2.3.1.5) | protein | 281 | 30% helix, 29% strand | Q5YYQ3 |
| C | Putative acetyltransferase (EC 2.3.1.5) | protein | 282 | 31% helix, 28% strand | Q5YYQ3 |
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 483 | 0.78 | 0.86 | 71 | empty |
| 2 | 549 | 0.77 | 0.84 | 77 | empty |
| 3 | 1060 | 0.77 | 0.79 | 86 | empty |
| 4 | 650 | 0.73 | 0.79 | 66 | empty |
| 5 | 351 | 0.67 | 0.81 | 36 | empty |
Interfaces
4 interfaces between chains.
- C–D · 1405 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1337 Ų buried · 16 hydrogen bonds · protein-protein
- B–D · 463 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 191 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3D9W · Crystal Structure Analysis of Nocardia farcinica Arylamine N-acetyltransferase · 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 Q5YYQ3
- Elsewhere: RCSB PDB 3D9W · PDBe 3D9W · UniProt Q5YYQ3
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