MolNFT v1 · #161888 · protein
Crystal structure of human angiotensin-1 converting enzyme N-domain in complex with bppb
6QS1 · Angiotensin-converting enzyme: “Crystal structure of human angiotensin-1 converting enzyme N-domain in complex with bppb”. X-ray diffraction, 7 ligands (NAG, FUC, BMA), 11 pockets (best druggability 0.86). MolNFT v1 #161888 on…
- PDB
- 6QS1
- Type
- protein
- Length
- 1,227 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Angiotensin-converting enzyme; Bradykinin potentiating peptide B
- EC
- 3.2.1.-, 3.4.15.1
- UniProt
- P12821
- Ligands
- NAG, FUC, BMA, ZN, MG, BO3, CL
- Pockets
- 11 · best druggability 0.86
Structure
x-ray diffraction · 4 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 | 63% helix, 3% strand | P12821 |
| B | Angiotensin-converting enzyme (EC 3.2.1.-, 3.4.15.1) | protein | 603 | 62% helix, 3% strand | P12821 |
| E | Bradykinin potentiating peptide B | protein | 11 | 0% helix, 9% strand | — |
| F | Bradykinin potentiating peptide B | protein | 5 | 0% helix, 20% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A, B
- FUC · alpha-L-fucopyranose · sugar · 4 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · chains A
- ZN · Zinc ion · metal · 2 copies · chains A, E, B, F
- MG · Magnesium ion · metal · 2 copies · chains A, B
- BO3 · Boric acid · ion · 7 copies · chains A, B
- CL · Chloride ion · ion · 4 copies · chains A, E, B, F
- EDO · 1,2-ethanediol · additive · 6 copies · chains A, E, B
- PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, B
- XPE · 3,6,9,12,15,18,21,24,27-nonaoxanonacosane-1,29-diol · additive · chains A
- PGE · Triethylene glycol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 813 | 0.86 | 0.88 | 83 | EDO, CL |
| 2 | 1147 | 0.84 | 0.85 | 77 | EDO, CL |
| 3 | 491 | 0.83 | 0.90 | 78 | MG |
| 4 | 466 | 0.83 | 0.90 | 74 | MG |
| 5 | 237 | 0.76 | 0.90 | 32 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1079 Ų buried · 14 hydrogen bonds · protein-protein
- A–E · 997 Ų buried · 18 hydrogen bonds · protein-protein
- B–F · 523 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 6 glycan, 1 modified (disulfide, N-glycosylation, cyclization).
Compared structures
- 6QS1 · Crystal structure of human Angiotensin-1 converting enzyme N-domain in complex with BPPb · 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 6QS1 · PDBe 6QS1 · UniProt P12821
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