Research workbench
Crystal structure of AQ_1058, a transcriptional regulator (TERR/ACRR family) from aquifex aeolicus VF5
Analyse Crystal structure of AQ_1058, a transcriptional regulator (TERR/ACRR family)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EH3
- Type
- protein
- Length
- 171 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator
- UniProt
- O67157
- Ligands
- MG
- Pockets
- 1 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator | protein | 171 | 81% helix, 0% strand | O67157 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 218 | 0.79 | 0.92 | 22 | empty |
Modifications
Observed in the structure: 1 modified (engineered).
Compared structures
- 2EH3 · Crystal structure of aq_1058, a transcriptional regulator (TerR/AcrR family) from Aquifex… · the same entry in another collection · chain A against A, TM-score 1.00
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 O67157
- Elsewhere: RCSB PDB 2EH3 · PDBe 2EH3 · UniProt O67157
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