Research workbench
Crystal structure of lhk-exo in complex with damp
Analyse Crystal structure of lhk-exo in complex with damp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SZ4
- Type
- protein
- Length
- 195 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exonuclease
- UniProt
- C1D7P6
- Ligands
- D5M, MG
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exonuclease | protein | 195 | 57% helix, 16% strand | C1D7P6 |
Ligands and binding sites
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 | 350 | 0.55 | 0.74 | 43 | MG, D5M |
| 2 | 54 | 0.38 | 0.81 | 14 | empty |
Compared structures
- 3SZ4 · Crystal Structure of LHK-Exo in complex with dAMP · 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 C1D7P6
- Elsewhere: RCSB PDB 3SZ4 · PDBe 3SZ4 · UniProt C1D7P6
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