Research workbench
Crystal structure of alfa carbonic anhydrase from Schistosoma mansoni with 4-(2-(3-(4-iodophenyl)ureido)ethyl)benzenesulfonamide
Analyse Crystal structure of alfa carbonic anhydrase from Schistosoma mansoni with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OA1
- Type
- protein
- Length
- 554 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Schistosoma mansoni
- Molecule
- Carbonic anhydrase
- EC
- 4.2.1.1
- UniProt
- A0A3Q0KSG2
- Ligands
- TKQ, NAG, ZN
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 16% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| AAA, BBB | Carbonic anhydrase (EC 4.2.1.1) | protein | 277 | 16% helix, 29% strand | A0A3Q0KSG2 |
Ligands and binding sites
- TKQ · 1-(4-iodophenyl)-3-[2-(4-sulfamoylphenyl)ethyl]urea · ligand · 2 copies · chains AAA, BBB
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains BBB, AAA
- ZN · Zinc ion · metal · 2 copies · chains AAA, BBB
- GOL · Glycerol · additive · chains AAA, BBB
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.75 | 0.97 | 37 | GOL |
| 2 | 464 | 0.64 | 0.77 | 67 | empty |
| 3 | 156 | 0.54 | 0.80 | 24 | TKQ |
| 4 | 127 | 0.54 | 0.82 | 24 | TKQ |
| 5 | 50 | 0.27 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- AAA–BBB · 1159 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 glycan, 2 disulfide (glycosylation, disulfide).
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 A0A3Q0KSG2
- Elsewhere: RCSB PDB 7OA1 · PDBe 7OA1 · UniProt A0A3Q0KSG2
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