Research workbench
Crystal structure of chaperone protein papd reveals an immunoglobulin fold
Analyse Crystal structure of chaperone protein papd reveals an immunoglobulin fold in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DPA
- Type
- protein
- Length
- 218 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein papd
- UniProt
- P15319
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein papd | protein | 218 | 0% helix, 0% strand | P15319 |
Compared structures
- 3DPA · Crystal structure of chaperone protein papd reveals an immunoglobulin fold · the same entry in another collection · chain A against A, TM-score 1.00
- P15319 · AlphaFold monomer V2.0 prediction for chaperone protein papd (P15319) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P15319
- Elsewhere: RCSB PDB 3DPA · PDBe 3DPA · UniProt P15319
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