Research workbench
Backbone Modification in the GA Module of Protein PAB: ACPC residues at positions 22 and 26
Analyse Backbone Modification in the GA Module of Protein PAB: ACPC residues at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 9BB5
- Type
- protein
- Length
- 47 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- NOT
- Molecule
- Peptostreptococcal albumin-binding protein
- UniProt
- Q51911
Structure
solution nmr · resolution NOT · 1 distinct chain · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptostreptococcal albumin-binding protein | protein | 47 | 77% helix, 0% strand | Q51911 |
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- Q51911 · AlphaFold monomer V2.0 prediction for peptostreptococcal albumin- binding protein (Q51911) · a predicted model of the same protein · chain A against A, TM-score 0.86
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 Q51911
- Elsewhere: RCSB PDB 9BB5 · PDBe 9BB5 · UniProt Q51911
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