MolNFT v1 · #135286 · protein
Crystal structure of the complex of helicobacter pylori alpha-carbonic anhydrase with 5-amino-1,3,4-thiadiazole-2-sulfonamide inhibitor.
5TUO: “Crystal structure of the complex of helicobacter pylori alpha-carbonic anhydrase with…”. X-ray diffraction, 3 ligands (1SA, ZN, CL), 20 pockets (best druggability 0.76). MolNFT v1 #135286 on GenesisL1: 3D structure, binding sites…
- PDB
- 5TUO
- Type
- protein
- Length
- 1,755 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-carbonic anhydrase
- EC
- 4.2.1.1
- UniProt
- A0A0M3KL20
- Ligands
- 1SA, ZN, CL
- Pockets
- 20 · best druggability 0.76
Structure
x-ray diffraction · 8 distinct chains · 14% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-carbonic anhydrase (EC 4.2.1.1) | protein | 224 | 15% helix, 38% strand | A0A0M3KL20 |
| B | Alpha-carbonic anhydrase (EC 4.2.1.1) | protein | 217 | 15% helix, 39% strand | A0A0M3KL20 |
| C | Alpha-carbonic anhydrase (EC 4.2.1.1) | protein | 226 | 13% helix, 38% strand | A0A0M3KL20 |
| D | Alpha-carbonic anhydrase (EC 4.2.1.1) | protein | 218 | 16% helix, 39% strand | A0A0M3KL20 |
| E | Alpha-carbonic anhydrase (EC 4.2.1.1) | protein | 228 | 15% helix, 39% strand | A0A0M3KL20 |
| F | Alpha-carbonic anhydrase (EC 4.2.1.1) | protein | 199 | 11% helix, 38% strand | A0A0M3KL20 |
| G | Alpha-carbonic anhydrase (EC 4.2.1.1) | protein | 225 | 16% helix, 36% strand | A0A0M3KL20 |
| H | Alpha-carbonic anhydrase (EC 4.2.1.1) | protein | 218 | 14% helix, 39% strand | A0A0M3KL20 |
Ligands and binding sites
- 1SA · 5-amino-1,3,4-thiadiazole-2-sulfonamide · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- ZN · Zinc ion · metal · 8 copies · chains A, B, C, D, E, F, G, H
- CL · Chloride ion · ion · 7 copies · chains A, B, C, D, E, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1182 | 0.76 | 0.79 | 106 | empty |
| 2 | 778 | 0.69 | 0.76 | 59 | empty |
| 3 | 405 | 0.65 | 0.79 | 53 | empty |
| 4 | 199 | 0.59 | 0.81 | 26 | 1SA |
| 5 | 187 | 0.58 | 0.81 | 24 | ZN, 1SA |
Interfaces
14 interfaces between chains.
- C–D · 1357 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1338 Ų buried · 22 hydrogen bonds · protein-protein
- G–H · 1334 Ų buried · 17 hydrogen bonds · protein-protein
- E–F · 1323 Ų buried · 22 hydrogen bonds · protein-protein
- A–F · 344 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 5TUO · Crystal structure of the complex of Helicobacter pylori alpha-carbonic anhydrase with… · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A0M3KL20
- Elsewhere: RCSB PDB 5TUO · PDBe 5TUO · UniProt A0A0M3KL20
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