Research workbench
Crystal structure of the extracellular domain of human carbonic anhydrase XII
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
- 1JCZ
- Type
- protein
- Length
- 520 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
- ZN
- Pockets
- 6 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Carbonic anhydrase XII (EC 4.2.1.1) | protein | 260 | 15% helix, 32% strand | O43570 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 330 | 0.78 | 0.89 | 51 | empty |
| 2 | 484 | 0.74 | 0.83 | 61 | empty |
| 3 | 200 | 0.56 | 0.79 | 27 | ACY |
| 4 | 158 | 0.54 | 0.80 | 28 | ACY |
| 5 | 154 | 0.51 | 0.79 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1247 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1JCZ · Crystal structure of the extracellular domain of human carbonic anhydrase XII · 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 1JCZ · PDBe 1JCZ · UniProt O43570
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