Research workbench
Cypa complexed with hvgpia (pseudo-symmetric monomer)
Analyse Cypa complexed with hvgpia (pseudo-symmetric monomer) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AWU
- Type
- protein
- Length
- 170 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclophilin a; Peptide from the HIV-1 capsid protein
- EC
- 5.2.1.8
- UniProt
- P62937
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclophilin a (EC 5.2.1.8) | protein | 164 | 14% helix, 32% strand | P62937 |
| B | Peptide from the HIV-1 capsid protein | protein | 6 | 0% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–B · 436 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1AWU · Cypa complexed with hvgpia (pseudo-symmetric monomer) · 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 1AWU · PDBe 1AWU · UniProt P62937
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.