Research workbench
Crystal structure of antitermination protein Q from bacteriophage lambda. northeast structural genomics consortium target OR18A.
Analyse Crystal structure of antitermination protein Q from bacteriophage lambda.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MO1
- Type
- protein
- Length
- 288 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Antitermination protein Q
- UniProt
- P03047
- Ligands
- ZN, BR, CL
- Pockets
- 5 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 64% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Antitermination protein Q | protein | 145 | 64% helix, 6% strand | P03047 |
| B | Antitermination protein Q | protein | 143 | 63% helix, 6% strand | P03047 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
- BR · Bromide ion · ion · 3 copies · chains A, B
- CL · Chloride ion · ion · 3 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.60 | 0.85 | 26 | BR |
| 2 | 191 | 0.48 | 0.75 | 20 | BR |
| 3 | 109 | 0.37 | 0.74 | 20 | empty |
| 4 | 64 | 0.31 | 0.75 | 12 | BR |
| 5 | 54 | 0.27 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 626 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 4MO1 · Crystal structure of antitermination protein Q from bacteriophage lambda. Northeast… · 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 P03047
- Elsewhere: RCSB PDB 4MO1 · PDBe 4MO1 · UniProt P03047
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