Research workbench
Atomic resolution structure of human carbonic anhydrase II in complex with furosemide
Analyse Atomic resolution structure of human carbonic anhydrase II in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SG0
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00918
- Ligands
- BE7, FUN, HG, NA, ZN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 257 | — | P00918 |
Ligands and binding sites
- BE7 · (4-carboxyphenyl)(chloro)mercury · ligand · chains A
- FUN · 5-(aminosulfonyl)-4-chloro-2-[(2-furylmethyl) amino]benzoic acid · ligand · chains A
- HG · Mercury (II) ion · metal · 2 copies · chains A
- NA · Sodium ion · metal · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6SG0 · Atomic resolution structure of Human Carbonic Anhydrase II in complex with furosemide · 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 6SG0 · PDBe 6SG0 · UniProt P00918
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