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Crystal structure of an anti-ecfsigma factor, chrr (MAQU_0586) from marinobacter aquaeolei VT8 at 1.70 a resolution
Analyse Crystal structure of an anti-ecfsigma factor, chrr (MAQU_0586) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3O14
- Type
- protein
- Length
- 444 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-ecfsigma factor, chrr
- UniProt
- A1TY68
- Ligands
- NIO, ZN, SO4
- Pockets
- 7 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Anti-ecfsigma factor, chrr | protein | 222 | 3% helix, 55% strand | A1TY68 |
Ligands and binding sites
- NIO · Nicotinic acid · ligand · chains A
- ZN · Zinc ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 16 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 636 | 0.77 | 0.83 | 73 | EDO, SO4 |
| 2 | 267 | 0.63 | 0.80 | 31 | NIO |
| 3 | 278 | 0.60 | 0.79 | 27 | empty |
| 4 | 53 | 0.40 | 0.82 | 16 | empty |
| 5 | 89 | 0.39 | 0.77 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 758 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 3O14 · Crystal structure of an anti-ECFsigma factor, ChrR (Maqu_0586) from MARINOBACTER… · 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 A1TY68
- Elsewhere: RCSB PDB 3O14 · PDBe 3O14 · UniProt A1TY68
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