MolNFT v2 · #177831 · protein
Structural insights into novel mechanisms of inhibition of the major b-carbonic anhydrase CafB from the pathogenic fungus Aspergillus fumigatus (disulfide-bonded form)
7CXX: “Structural insights into novel mechanisms of inhibition of the major b-carbonic anhydrase CafB from the…”. X-ray diffraction at 2, 1 ligand (SO4). MolNFT v2 #177831 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7CXX
- Type
- protein
- Length
- 417 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
- UniProt
- A4DA32
- Ligands
- SO4
Structure
x-ray diffraction · resolution 2 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 216 | — | A4DA32 |
| B | — | protein | 201 | — | A4DA32 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7CXX · Structural insights into novel mechanisms of inhibition of the major B-carbonic anhydrase… · the same entry in another collection · 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 A4DA32
- Elsewhere: RCSB PDB 7CXX · PDBe 7CXX · UniProt A4DA32
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