Research workbench
Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions
Analyse Crystallographic studies of the binding of protonated and unprotonated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CAO
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase II
- EC
- 4.2.1.1
- UniProt
- P00918
- Ligands
- ACE, ZN, H2S
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase II (EC 4.2.1.1) | protein | 259 | 16% helix, 31% strand | P00918 |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A
- ZN · Zinc ion · metal · chains A
- H2S · Hydrosulfuric acid · ion · chains A
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 | 127 | 0.56 | 0.83 | 27 | H2S |
| 2 | 52 | 0.26 | 0.74 | 13 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1CAO · Crystallographic studies of the binding of protonated and unprotonated inhibitors to… · the same entry in another collection · chain A against A, TM-score 1.00
- P00918 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 2 (P00918) · a predicted model of the same protein · chain A 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 1CAO · PDBe 1CAO · UniProt P00918
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