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Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
Analyse Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TE3
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Homo sapiens
- Molecule
- Carbonic anhydrase II
- EC
- 4.2.1.1
- UniProt
- P00918
- Ligands
- ZN, CL
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 16% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Carbonic anhydrase II (EC 4.2.1.1) | protein | 258 | 16% helix, 30% strand | P00918 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 101 | 0.53 | 0.83 | 24 | CL |
Compared structures
- 1TE3 · Effect of shuttle location and pH environment on H+ transfer in human carbonic anhydrase… · the same entry in another collection · chain X against X, TM-score 1.00
- P00918 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 2 (P00918) · a predicted model of the same protein · chain X 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 1TE3 · PDBe 1TE3 · UniProt P00918
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