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Crystal structure of drosophila ance
Analyse Crystal structure of drosophila ance in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1J38
- Type
- protein
- Length
- 1,196 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Angiotensin converting enzyme
- EC
- 3.4.15.1
- UniProt
- Q10714
- Ligands
- ZN
- Pockets
- 8 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Angiotensin converting enzyme (EC 3.4.15.1) | protein | 598 | 59% helix, 4% strand | Q10714 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1162 | 0.87 | 0.88 | 124 | empty |
| 2 | 551 | 0.85 | 0.91 | 72 | empty |
| 3 | 531 | 0.65 | 0.76 | 50 | empty |
| 4 | 74 | 0.56 | 0.87 | 10 | empty |
| 5 | 72 | 0.47 | 0.83 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 525 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
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 Q10714
- Elsewhere: RCSB PDB 1J38 · PDBe 1J38 · UniProt Q10714
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