Research workbench
Complex structure of esterase rppe S159A/W187H and substrate (S)-ac- cpa
Analyse Complex structure of esterase rppe S159A/W187H and substrate (S)-ac- cpa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OB6
- Type
- protein
- Length
- 319 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ALPHA/BETA hydrolase fold-3 domain protein
- EC
- 3.1.1.-
- UniProt
- L7PYQ2
- Ligands
- S2T
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ALPHA/BETA hydrolase fold-3 domain protein (EC 3.1.1.-) | protein | 319 | 43% helix, 21% strand | L7PYQ2 |
Ligands and binding sites
- S2T · (2S)-(acetyloxy)(2-chlorophenyl)ethanoic acid · ligand · 3 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 | 288 | 0.69 | 0.83 | 42 | S2T |
| 2 | 57 | 0.31 | 0.76 | 15 | empty |
Compared structures
- 4OB6 · Complex structure of esterase rPPE S159A/W187H and substrate (S)-Ac-CPA · 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 L7PYQ2
- Elsewhere: RCSB PDB 4OB6 · PDBe 4OB6 · UniProt L7PYQ2
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