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Crystal structure of BAP31 vded at acidic pH
Analyse Crystal structure of BAP31 vded at acidic pH in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JZP
- Type
- protein
- Length
- 102 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- B-cell receptor-associated protein 31
- UniProt
- P51572
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 94% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | B-cell receptor-associated protein 31 | protein | 52 | 96% helix, 0% strand | P51572 |
| B | B-cell receptor-associated protein 31 | protein | 50 | 92% helix, 0% strand | P51572 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1286 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
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 P51572
- Elsewhere: RCSB PDB 4JZP · PDBe 4JZP · UniProt P51572
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