Research workbench
The origin of the hydrophobic effect in the molecular recognition of arylsulfonamides by carbonic anhydrase
Analyse The origin of the hydrophobic effect in the molecular recognition of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3S78
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase 2
- EC
- 4.2.1.1
- UniProt
- P00918
- Ligands
- EVJ, ZN
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 258 | 15% helix, 30% strand | P00918 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 144 | 0.57 | 0.82 | 26 | EVJ |
| 2 | 57 | 0.28 | 0.74 | 15 | empty |
Compared structures
- 3S78 · The origin of the hydrophobic effect in the molecular recognition of arylsulfonamides by… · the same entry in another collection · chain B against B, TM-score 1.00
- P00918 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 2 (P00918) · 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 P00918
- Elsewhere: RCSB PDB 3S78 · PDBe 3S78 · UniProt P00918
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.