MolNFT v2 · #119878 · protein
An unusual natural product primary sulfonamide: synthesis, carbonic anhydrase inhibition and protein x-ray structure of Psammaplin C
5G03: “An unusual natural product primary sulfonamide: synthesis, carbonic anhydrase inhibition and protein x-ray…”. X-ray diffraction at 1.35, 3 ligands (OE2, ZN, SO4). MolNFT v2 #119878 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5G03
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.35
- Source
- HOMO SAPIENS
- UniProt
- P00918
- Ligands
- OE2, ZN, SO4
Structure
x-ray diffraction · resolution 1.35 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 257 | — | P00918 |
Ligands and binding sites
- OE2 · Psammaplin C · ligand · chains A
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5G03 · An unusual natural product primary sulfonamide: synthesis, carbonic anhydrase inhibition… · 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 5G03 · PDBe 5G03 · UniProt P00918
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