MolNFT v1 · #6726 · protein
Crystal structure of S-glutathiolated carbonic anhydrase III
1FLJ: “Crystal structure of S-glutathiolated carbonic anhydrase III”. X-ray diffraction, 3 ligands (GSH, ACE, ZN), 2 pockets (best druggability 0.54). MolNFT v1 #6726 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1FLJ
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase III
- EC
- 4.2.1.1
- UniProt
- P14141
- Ligands
- GSH, ACE, ZN
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase III (EC 4.2.1.1) | protein | 259 | 18% helix, 30% strand | P14141 |
Ligands and binding sites
- GSH · Glutathione · ligand · 2 copies · chains A
- ACE · Acetyl group · ligand · chains A
- ZN · Zinc ion · metal · 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 | 165 | 0.54 | 0.80 | 28 | empty |
| 2 | 87 | 0.34 | 0.74 | 19 | empty |
Modifications
Observed in the structure: 3 covalent (covalent ligand).
Compared structures
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 P14141
- Elsewhere: RCSB PDB 1FLJ · PDBe 1FLJ · UniProt P14141
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