Research workbench
Crystal structure of the extracellular domain of human carbonic anhydrase XII complexed with acetazolamide
Analyse Crystal structure of the extracellular domain of human carbonic anhydrase XII… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JD0
- Type
- protein
- Length
- 519 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase XII
- EC
- 4.2.1.1
- UniProt
- O43570
- Ligands
- AZM, ZN
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase XII (EC 4.2.1.1) | protein | 260 | 15% helix, 32% strand | O43570 |
| B | Carbonic anhydrase XII (EC 4.2.1.1) | protein | 259 | 16% helix, 32% strand | O43570 |
Ligands and binding sites
- AZM · 5-acetamido-1,3,4-thiadiazole-2-sulfonamide · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 305 | 0.78 | 0.90 | 46 | empty |
| 2 | 340 | 0.71 | 0.83 | 44 | empty |
| 3 | 286 | 0.65 | 0.82 | 33 | empty |
| 4 | 211 | 0.58 | 0.80 | 29 | AZM |
| 5 | 204 | 0.56 | 0.79 | 25 | AZM |
Interfaces
1 interface between chains.
- A–B · 1242 Ų buried · 29 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1JD0 · Crystal structure of the extracellular domain of human carbonic anhydrase XII complexed… · the same entry in another collection · chain A against A, TM-score 1.00
- O43570 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 12 (O43570) · a predicted model of the same protein · 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 O43570
- Elsewhere: RCSB PDB 1JD0 · PDBe 1JD0 · UniProt O43570
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