Research workbench
Cyclophilin a complexed with a fragment of crk-II
Analyse Cyclophilin a complexed with a fragment of crk-II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MS4
- Type
- protein
- Length
- 174 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase a; Peptide
- EC
- 5.2.1.8
- UniProt
- P62937
Structure
solution nmr · 2 distinct chains · 13% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8) | protein | 165 | 14% helix, 34% strand | P62937 |
| B | Peptide | protein | 9 | 0% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–B · 473 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2MS4 · Cyclophilin a complexed with a fragment of crk-ii · 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 2MS4 · PDBe 2MS4 · UniProt P62937
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