Research workbench
Crystal structure of the complex of helicobacter pylori alpha-carbonic anhydrase with ethoxzolamide
Analyse Crystal structure of the complex of helicobacter pylori alpha-carbonic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TT3
- Type
- protein
- Length
- 1,751 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-carbonic anhydrase
- UniProt
- A0A0M3KL20
- Ligands
- EZL, ZN, CL
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 8 distinct chains · 15% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-carbonic anhydrase | protein | 223 | 15% helix, 39% strand | A0A0M3KL20 |
| B | Alpha-carbonic anhydrase | protein | 212 | 12% helix, 39% strand | A0A0M3KL20 |
| C | Alpha-carbonic anhydrase | protein | 227 | 16% helix, 39% strand | A0A0M3KL20 |
| D | Alpha-carbonic anhydrase | protein | 202 | 14% helix, 34% strand | A0A0M3KL20 |
| E | Alpha-carbonic anhydrase | protein | 226 | 15% helix, 40% strand | A0A0M3KL20 |
| F | Alpha-carbonic anhydrase | protein | 220 | 15% helix, 39% strand | A0A0M3KL20 |
| G | Alpha-carbonic anhydrase | protein | 218 | 13% helix, 39% strand | A0A0M3KL20 |
| H | Alpha-carbonic anhydrase | protein | 223 | 15% helix, 39% strand | A0A0M3KL20 |
Ligands and binding sites
- EZL · 6-ethoxy-1,3-benzothiazole-2-sulfonamide · ligand · 7 copies · chains A, B, C, E, F, G, H
- ZN · Zinc ion · metal · 8 copies · chains A, B, C, D, E, F, G, H
- CL · Chloride ion · ion · 6 copies · chains A, B, C, E, G, H
- GOL · Glycerol · additive · 5 copies · chains A, B, C, E, 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 | 998 | 0.79 | 0.81 | 91 | empty |
| 2 | 939 | 0.75 | 0.78 | 84 | empty |
| 3 | 64 | 0.71 | 0.97 | 23 | empty |
| 4 | 721 | 0.68 | 0.76 | 56 | empty |
| 5 | 227 | 0.63 | 0.82 | 30 | empty |
Interfaces
16 interfaces between chains.
- C–D · 1406 Ų buried · 20 hydrogen bonds · protein-protein
- G–H · 1331 Ų buried · 23 hydrogen bonds · protein-protein
- E–F · 1296 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 1289 Ų buried · 15 hydrogen bonds · protein-protein
- A–F · 503 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 5TT3 · 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 5TT3 · PDBe 5TT3 · UniProt A0A0M3KL20
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