Research workbench
Crystal structure of pas domain of S. aureus yycg
Analyse Crystal structure of pas domain of S. aureus yycg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MN5
- Type
- protein
- Length
- 204 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor protein kinase walk
- EC
- 2.7.13.3
- UniProt
- Q9RDT3
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensor protein kinase walk (EC 2.7.13.3) | protein | 103 | 17% helix, 35% strand | Q9RDT3 |
| B | Sensor protein kinase walk (EC 2.7.13.3) | protein | 101 | 20% helix, 35% strand | Q9RDT3 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, 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 | 96 | 0.36 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 876 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
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 Q9RDT3
- Elsewhere: RCSB PDB 4MN5 · PDBe 4MN5 · UniProt Q9RDT3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.