Research workbench
Crystal structure of pzp domain of human AF10 protein fused with histone H3 peptide
Analyse Crystal structure of pzp domain of human AF10 protein fused with histone H3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DAH
- Type
- protein
- Length
- 378 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P55197
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 179 | — | P55197 |
| B | — | protein | 181 | — | P55197 |
| C, D | — | protein | 9 | — | — |
Compared structures
- 5DAH · Crystal structure of PZP domain of human AF10 protein fused with Histone H3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P55197 · AlphaFold monomer V2.0 prediction for protein af-10 (P55197) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P55197
- Elsewhere: RCSB PDB 5DAH · PDBe 5DAH · UniProt P55197
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