Research workbench
Crystal structure of the lipoteichoic acid synthase ltap from listeria monocytogenes
Analyse Crystal structure of the lipoteichoic acid synthase ltap from listeria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UOP
- Type
- protein
- Length
- 817 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipoteichoic acid primase
- EC
- 2.7.8.-
- UniProt
- Q8Y989
- Ligands
- MG, CL
- Pockets
- 4 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipoteichoic acid primase (EC 2.7.8.-) | protein | 408 | 36% helix, 17% strand | Q8Y989 |
| B | Lipoteichoic acid primase (EC 2.7.8.-) | protein | 409 | 37% helix, 17% strand | Q8Y989 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 3 copies · chains B
- 1PE · Pentaethylene glycol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1190 | 0.82 | 0.83 | 110 | empty |
| 2 | 123 | 0.69 | 0.91 | 29 | empty |
| 3 | 218 | 0.57 | 0.79 | 24 | empty |
| 4 | 231 | 0.56 | 0.78 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 1129 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 4UOP · Crystal structure of the lipoteichoic acid synthase LtaP from Listeria monocytogenes · 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 Q8Y989
- Elsewhere: RCSB PDB 4UOP · PDBe 4UOP · UniProt Q8Y989
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