Research workbench
Structure and inhibition of the CO2-sensing carbonic anhydrase CAN2 from the pathogenic fungus cryptococcus neoformans
Analyse Structure and inhibition of the CO2-sensing carbonic anhydrase CAN2 from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W3N
- Type
- protein
- Length
- 680 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase 2
- EC
- 4.2.1.1
- UniProt
- Q3I4V7
- Ligands
- ZN
- Pockets
- 7 · best druggability 0.63
Structure
x-ray diffraction · 3 distinct chains · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 230 | 47% helix, 14% strand | Q3I4V7 |
| B | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 225 | 46% helix, 14% strand | Q3I4V7 |
| C | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 225 | 50% helix, 14% strand | Q3I4V7 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A, B, C
- ACT · Acetate ion · additive · 3 copies · chains A, B, C
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.63 | 0.94 | 20 | empty |
| 2 | 80 | 0.44 | 0.81 | 23 | empty |
| 3 | 131 | 0.40 | 0.74 | 22 | empty |
| 4 | 118 | 0.37 | 0.74 | 19 | empty |
| 5 | 51 | 0.36 | 0.80 | 18 | empty |
Interfaces
3 interfaces between chains.
- B–C · 3750 Ų buried · 44 hydrogen bonds · protein-protein
- A–B · 304 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 152 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2W3N · Structure and inhibition of the CO2-sensing carbonic anhydrase Can2 from the pathogenic… · 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 Q3I4V7
- Elsewhere: RCSB PDB 2W3N · PDBe 2W3N · UniProt Q3I4V7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.