Research workbench
Sm Endonuclease from Seratia marcenscens at atomic resolution
Analyse Sm Endonuclease from Seratia marcenscens at atomic resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QL0
- Type
- protein
- Length
- 482 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.1
- Source
- SERRATIA MARCESCENS
- Molecule
- Nuclease
- EC
- 3.1.30.2
- UniProt
- P13717
- Ligands
- MG
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · resolution 1.1 · 1 distinct chain · 27% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Nuclease (EC 3.1.30.2) | protein | 241 | 27% helix, 22% strand | P13717 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains B, A
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 | 62 | 0.34 | 0.77 | 19 | MG |
Interfaces
1 interface between chains.
- A–B · 928 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 P13717
- Elsewhere: RCSB PDB 1QL0 · PDBe 1QL0 · UniProt P13717
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