Research workbench
Crystal structure of yersinia pestis lsrg
Analyse Crystal structure of yersinia pestis lsrg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GFF
- Type
- protein
- Length
- 197 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lsrg protein
- Ligands
- CL
- Pockets
- 3 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lsrg protein | protein | 97 | 40% helix, 37% strand | — |
| B | Lsrg protein | protein | 100 | 38% helix, 36% strand | — |
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
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 107 | 0.61 | 0.86 | 21 | empty |
| 2 | 78 | 0.53 | 0.85 | 18 | empty |
| 3 | 53 | 0.27 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1193 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 2GFF · Crystal Structure of Yersinia pestis LsrG · the same entry in another collection · chain B against B, 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
- Elsewhere: RCSB PDB 2GFF · PDBe 2GFF
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