Research workbench
Lytr-CPS2A-psr family protein with bound octaprenyl pyrophosphate lipid and manganese ion
Analyse Lytr-CPS2A-psr family protein with bound octaprenyl pyrophosphate lipid and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TEL
- Type
- protein
- Length
- 372 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CPS2A, integral membrane regulatory protein wzg
- UniProt
- Q4K376
- Ligands
- ZTP, MN
- Pockets
- 3 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CPS2A, integral membrane regulatory protein wzg | protein | 372 | 39% helix, 28% strand | Q4K376 |
Ligands and binding sites
- ZTP · (2Z,6Z,10Z,14Z,18Z,22Z,26Z)-3,7,11,15,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaen-1-yl trihydrogen diphosphate · ligand · chains A
- MN · Manganese (II) ion · metal · chains A
- ACT · Acetate ion · additive · 4 copies · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 832 | 0.86 | 0.88 | 64 | ZTP, EDO |
| 2 | 352 | 0.61 | 0.78 | 43 | empty |
| 3 | 60 | 0.49 | 0.86 | 21 | EDO |
Compared structures
- 3TEL · LytR-CPS2A-Psr family protein with bound octaprenyl pyrophosphate lipid and manganese ion · 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 Q4K376
- Elsewhere: RCSB PDB 3TEL · PDBe 3TEL · UniProt Q4K376
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