Research workbench
Iaa acetyltransferase from bacillus cereus atcc 14579
Analyse Iaa acetyltransferase from bacillus cereus atcc 14579 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Y9K
- Type
- protein
- Length
- 609 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Iaa acetyltransferase
- EC
- 2.3.1.-
- UniProt
- Q81FK8
- Pockets
- 10 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 33% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Iaa acetyltransferase (EC 2.3.1.-) | protein | 152 | 34% helix, 36% strand | Q81FK8 |
| B | Iaa acetyltransferase (EC 2.3.1.-) | protein | 154 | 31% helix, 35% strand | Q81FK8 |
| C | Iaa acetyltransferase (EC 2.3.1.-) | protein | 150 | 35% helix, 37% strand | Q81FK8 |
| D | Iaa acetyltransferase (EC 2.3.1.-) | protein | 153 | 34% helix, 37% strand | Q81FK8 |
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1127 | 0.84 | 0.84 | 103 | empty |
| 2 | 384 | 0.66 | 0.80 | 52 | empty |
| 3 | 364 | 0.66 | 0.80 | 45 | empty |
| 4 | 330 | 0.66 | 0.81 | 44 | empty |
| 5 | 342 | 0.65 | 0.80 | 45 | empty |
Interfaces
6 interfaces between chains.
- A–B · 602 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 592 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 208 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 185 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 175 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 23 modified (engineered).
Compared structures
- 1Y9K · IAA acetyltransferase from Bacillus cereus ATCC 14579 · 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 Q81FK8
- Elsewhere: RCSB PDB 1Y9K · PDBe 1Y9K · UniProt Q81FK8
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