Research workbench
Structural basis of inhibitor affinity to variants of human carbonic anhydrase II
Analyse Structural basis of inhibitor affinity to variants of human carbonic anhydrase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YDC
- Type
- protein
- Length
- 255 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
- ZN, HG
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase II (EC 4.2.1.1) | protein | 255 | 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 | 125 | 0.57 | 0.83 | 24 | empty |
Compared structures
- 1YDC · Structural basis of inhibitor affinity to variants of human carbonic anhydrase II · 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 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 P00918
- Elsewhere: RCSB PDB 1YDC · PDBe 1YDC · UniProt P00918
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