Research workbench
1.8 ångström crystal structure of signal peptidase I from bacillus anthracis.
Analyse 1.8 ångström crystal structure of signal peptidase I 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
- 4NV4
- Type
- protein
- Length
- 227 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Signal peptidase I
- EC
- 3.4.21.89
- UniProt
- Q81TW3
- Pockets
- 3 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal peptidase I (EC 3.4.21.89) | protein | 115 | 23% helix, 21% strand | Q81TW3 |
| B | Signal peptidase I (EC 3.4.21.89) | protein | 112 | 21% helix, 21% strand | Q81TW3 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · 3 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.47 | 0.76 | 22 | empty |
| 2 | 148 | 0.42 | 0.74 | 20 | empty |
| 3 | 81 | 0.32 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 252 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 4NV4 · 1.8 Angstrom Crystal Structure of Signal Peptidase I 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 Q81TW3
- Elsewhere: RCSB PDB 4NV4 · PDBe 4NV4 · UniProt Q81TW3
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