Research workbench
Crystal structure of cyclophilin B at 1.2 a resolution
Analyse Crystal structure of cyclophilin B at 1.2 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ICH
- Type
- protein
- Length
- 180 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase B
- EC
- 5.2.1.8
- UniProt
- P23284
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase B (EC 5.2.1.8) | protein | 180 | 13% helix, 37% strand | P23284 |
Compared structures
- 3ICH · Crystal structure of cyclophilin B at 1.2 A resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P23284 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase B (P23284) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P23284
- Elsewhere: RCSB PDB 3ICH · PDBe 3ICH · UniProt P23284
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