Research workbench
Crystal structure of angiotensin-1 converting enzyme N-domain in complex with dual ACE/NEP inhibitor AD011
Analyse Crystal structure of angiotensin-1 converting enzyme N-domain in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q24
- Type
- protein
- Length
- 1,215 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Angiotensin-converting enzyme
- EC
- 3.2.1.-, 3.4.15.1
- UniProt
- P12821
- Ligands
- 8KC, NAG, FUC, BMA, ZN, MG, CL
- Pockets
- 7 · best druggability 0.87
Structure
x-ray diffraction · 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 | 606 | 62% helix, 3% strand | P12821 |
| B | Angiotensin-converting enzyme (EC 3.2.1.-, 3.4.15.1) | protein | 609 | 62% helix, 3% strand | P12821 |
Ligands and binding sites
- 8KC · (2~{S})-2-[[(2~{S})-1-[[(2~{S})-3-(1~{H}-indol-3-yl)-1-oxidanyl-1-oxidanylidene-propan-2-yl]amino]-1-oxidanylidene-hexan-2-yl]amino]-4-phenyl-butanoic acid · ligand · 2 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A, B
- FUC · alpha-L-fucopyranose · sugar · 4 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
- ACT · Acetate ion · additive · 3 copies · chains A, B
- PG4 · Tetraethylene glycol · additive · 2 copies · chains A, B
- P33 · 3,6,9,12,15,18-hexaoxaicosane-1,20-diol · additive · chains A
- P6G · Hexaethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1135 | 0.87 | 0.88 | 129 | PEG, P6G, ZN, 8KC |
| 2 | 479 | 0.85 | 0.92 | 53 | MG, 8KC |
| 3 | 228 | 0.77 | 0.91 | 27 | empty |
| 4 | 629 | 0.73 | 0.80 | 56 | ACT, PG4 |
| 5 | 213 | 0.72 | 0.88 | 34 | PG4, EDO |
Interfaces
1 interface between chains.
- A–B · 1085 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 6 glycan (disulfide, N-glycosylation).
Compared structures
- 7Q24 · Crystal structure of Angiotensin-1 converting enzyme N-domain in complex with dual… · 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 7Q24 · PDBe 7Q24 · UniProt P12821
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