Research workbench
K428A muntant nuclease domain of the large terminase subunit GP2 of bacterial virus SF6 with manganese
Analyse K428A muntant nuclease domain of the large terminase subunit GP2 of bacterial… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5C15
- Type
- protein
- Length
- 224 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gene 2 protein
- UniProt
- Q716H3
- Ligands
- MN
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gene 2 protein | protein | 224 | 44% helix, 19% strand | Q716H3 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 167 | 0.52 | 0.79 | 26 | MN |
| 2 | 161 | 0.42 | 0.74 | 20 | empty |
Compared structures
- 5C15 · K428A mutant nuclease domain of the large terminase subunit gp2 of bacterial virus Sf6… · 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 Q716H3
- Elsewhere: RCSB PDB 5C15 · PDBe 5C15 · UniProt Q716H3
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