Research workbench
Monoclinic structure of P. aeruginosa ligd phosphoesterase domain
Analyse Monoclinic structure of P. aeruginosa ligd phosphoesterase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3N9D
- Type
- protein
- Length
- 148 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable ATP-dependent DNA ligase
- UniProt
- Q9I1X7
- Ligands
- YT3, MN, SO4
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable ATP-dependent DNA ligase | protein | 148 | 11% helix, 47% strand | Q9I1X7 |
Ligands and binding sites
- YT3 · Yttrium (III) ion · metal · 2 copies · chains A
- MN · Manganese (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3N9D · Monoclinic Structure of P. aeruginosa LigD phosphoesterase domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q9I1X7 · AlphaFold monomer V2.0 prediction for multifunctional non-homologous end joining protein… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q9I1X7
- Elsewhere: RCSB PDB 3N9D · PDBe 3N9D · UniProt Q9I1X7
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