Research workbench
1.5 ångström crystal structure of putative lipoprotein from bacillus anthracis.
Analyse 1.5 ångström crystal structure of putative lipoprotein from bacillus anthracis. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NOH
- Type
- protein
- Length
- 334 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipoprotein, putative
- UniProt
- Q81JR6
- Ligands
- CL
- Pockets
- 1 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Lipoprotein, putative | protein | 167 | 20% helix, 41% strand | Q81JR6 |
Ligands and binding sites
- CL · Chloride ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.45 | 0.75 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 650 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 4NOH · 1.5 Angstrom Crystal Structure of Putative Lipoprotein from Bacillus anthracis. · 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 Q81JR6
- Elsewhere: RCSB PDB 4NOH · PDBe 4NOH · UniProt Q81JR6
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