Research workbench
Crystal structure of human Angiotensin-1 converting enzyme N-domain in complex with Omapatrilat.
Analyse Crystal structure of human Angiotensin-1 converting enzyme N-domain in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H5X
- Type
- protein
- Length
- 1,214 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Homo sapiens
- Molecule
- Angiotensin-converting enzyme
- EC
- 3.2.1.-, 3.4.15.1
- UniProt
- P12821
- Ligands
- FT8, NAG, FUC, BMA, ZN, MG, CL
- Pockets
- 9 · best druggability 0.87
Structure
x-ray diffraction · resolution 1.8 · 2 distinct chains · 62% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Angiotensin-converting enzyme (EC 3.2.1.-, 3.4.15.1) | protein | 608 | 62% helix, 3% strand | P12821 |
| B | Angiotensin-converting enzyme (EC 3.2.1.-, 3.4.15.1) | protein | 606 | 62% helix, 3% strand | P12821 |
Ligands and binding sites
- FT8 · Omapatrilat · ligand · 2 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 11 copies · chains A, B
- FUC · alpha-L-fucopyranose · sugar · 4 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · chains B
- ZN · Zinc ion · metal · 2 copies · chains A, B
- MG · Magnesium ion · metal · chains B
- CL · Chloride ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 12 copies · chains A, B
- XPE · 3,6,9,12,15,18,21,24,27-nonaoxanonacosane-1,29-diol · additive · chains A
- PG4 · Tetraethylene glycol · additive · chains A, B
- PGE · Triethylene glycol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1158 | 0.87 | 0.88 | 117 | FT8, EDO |
| 2 | 435 | 0.85 | 0.92 | 54 | FT8 |
| 3 | 238 | 0.78 | 0.91 | 30 | empty |
| 4 | 847 | 0.76 | 0.80 | 52 | PG4 |
| 5 | 267 | 0.74 | 0.88 | 45 | EDO |
Interfaces
1 interface between chains.
- A–B · 1088 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 6 glycan (disulfide, N-glycosylation).
Compared structures
- 6H5X · Crystal structure of human angiotensin-1 converting enzyme N-domain in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P12821 · AlphaFold monomer V2.0 prediction for angiotensin-converting enzyme (P12821) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P12821
- Elsewhere: RCSB PDB 6H5X · PDBe 6H5X · UniProt P12821
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