Research workbench
Free acetyl-cypa orthorhombic form
Analyse Free acetyl-cypa orthorhombic form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X25
- Type
- protein
- Length
- 168 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase a
- EC
- 5.2.1.8
- UniProt
- P62937
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Peptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8) | protein | 168 | 14% helix, 33% strand | P62937 |
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 2X25 · Free acetyl-CypA orthorhombic form · the same entry in another collection · chain B against B, 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 2X25 · PDBe 2X25 · UniProt P62937
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