Research workbench
Ornithine aminotransferase PY00104 from plasmodium yoelii
Analyse Ornithine aminotransferase PY00104 from plasmodium yoelii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z7D
- Type
- protein
- Length
- 2,248 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ornithine aminotransferase
- EC
- 2.6.1.13
- UniProt
- Q7RT90
- Pockets
- 16 · best druggability 0.75
Structure
x-ray diffraction · 5 distinct chains · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ornithine aminotransferase (EC 2.6.1.13) | protein | 378 | 41% helix, 21% strand | Q7RT90 |
| B | Ornithine aminotransferase (EC 2.6.1.13) | protein | 377 | 41% helix, 20% strand | Q7RT90 |
| C | Ornithine aminotransferase (EC 2.6.1.13) | protein | 369 | 41% helix, 19% strand | Q7RT90 |
| D, F | Ornithine aminotransferase (EC 2.6.1.13) | protein | 375 | 39% helix, 20% strand | Q7RT90 |
| E | Ornithine aminotransferase (EC 2.6.1.13) | protein | 374 | 41% helix, 20% strand | Q7RT90 |
Pockets
16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 972 | 0.75 | 0.78 | 96 | empty |
| 2 | 665 | 0.73 | 0.79 | 75 | empty |
| 3 | 470 | 0.72 | 0.82 | 56 | empty |
| 4 | 671 | 0.67 | 0.76 | 70 | empty |
| 5 | 456 | 0.66 | 0.78 | 60 | empty |
Interfaces
6 interfaces between chains.
- E–F · 3917 Ų buried · 41 hydrogen bonds · protein-protein
- A–B · 3854 Ų buried · 41 hydrogen bonds · protein-protein
- C–D · 3845 Ų buried · 44 hydrogen bonds · protein-protein
- A–C · 352 Ų buried · 1 hydrogen bond · protein-protein
- A–E · 201 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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 Q7RT90
- Elsewhere: RCSB PDB 1Z7D · PDBe 1Z7D · UniProt Q7RT90
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