Research workbench
Bartonella henselae bepa fic domain in complex with its antitoxin homologue biaa
Analyse Bartonella henselae bepa fic domain in complex with its antitoxin homologue biaa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NH2
- Type
- protein
- Length
- 345 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenosine monophosphate-protein transferase; Uncharacterized protein
- EC
- 2.7.7.-
- UniProt
- Q6G2A9, A0A0H3LZG7
- Ligands
- MG
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosine monophosphate-protein transferase (EC 2.7.7.-) | protein | 289 | 47% helix, 13% strand | Q6G2A9 |
| B | Uncharacterized protein | protein | 56 | 71% helix, 0% strand | A0A0H3LZG7 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 470 | 0.68 | 0.79 | 50 | MG |
| 2 | 451 | 0.67 | 0.79 | 45 | empty |
| 3 | 51 | 0.42 | 0.83 | 16 | empty |
| 4 | 52 | 0.37 | 0.81 | 14 | empty |
| 5 | 51 | 0.34 | 0.78 | 9 | empty |
Interfaces
1 interface between chains.
- A–B · 1251 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 5NH2 · Bartonella henselae BepA Fic domain in complex with its antitoxin homologue BiaA · the same entry in another collection · chain A against A, TM-score 1.00
- Q6G2A9 · AlphaFold monomer V2.0 prediction for protein adenylyltransferase (Q6G2A9) · 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 Q6G2A9
- Every structure of UniProt A0A0H3LZG7
- Elsewhere: RCSB PDB 5NH2 · PDBe 5NH2 · UniProt Q6G2A9 · UniProt A0A0H3LZG7
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