Research workbench
X-ray structure of cypa-C52AK125C/CSA/AROMATIC foldamer complex
Analyse X-ray structure of cypa-C52AK125C/CSA/AROMATIC foldamer complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PCJ
- Type
- protein
- Length
- 350 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P62937
- Ligands
- QUK, 7I7, QVS, QUJ, 7IB
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 164 | — | P62937 |
| B, E | — | protein | 11 | — | — |
Ligands and binding sites
- QUK · 8-azanyl-4-(3-azanylpropoxy)quinoline-2-carboxylic acid · ligand · 4 copies · chains A, D
- 7I7 · N-[2-[2-[2-(2-formamidoethoxy)ethoxy]ethoxy]ethyl]-3-sulfanyl-propanamide · ligand · 2 copies · chains A, D
- QVS · 8-azanyl-4-oxidanyl-quinoline-2-carboxylic acid · ligand · 2 copies
- QUJ · 8-azanyl-4-(2-methylpropoxy)quinoline-2-carboxylic acid · ligand · 2 copies
- 7IB · 8-azanyl-5-(4-oxidanyl-4-oxidanylidene-butyl)quinoline-2-carboxylic acid · ligand · 2 copies · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7PCJ · X-ray structure of CypA-C52AK125C/CsA/aromatic foldamer complex · 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 P62937
- Elsewhere: RCSB PDB 7PCJ · PDBe 7PCJ · UniProt P62937
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