Research workbench
Microbial hormone-sensitive lipase E53 mutant S285G
Analyse Microbial hormone-sensitive lipase E53 mutant S285G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CIH
- Type
- protein
- Length
- 1,240 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A074MDU6
- Ligands
- D8F, NPO, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 309 | — | A0A074MDU6 |
| C, D | — | protein | 311 | — | A0A074MDU6 |
Ligands and binding sites
- D8F · (4-nitrophenyl) hexanoate · ligand · 4 copies · chains A, B, C, D
- NPO · P-nitrophenol · ligand · 2 copies · chains B
- SO4 · Sulfate ion · ion · 2 copies · chains B, D
- EDO · 1,2-ethanediol · additive · 18 copies · chains A, C, B, D
- DMS · Dimethyl sulfoxide · additive · 13 copies · chains A, C, B, D
- GOL · Glycerol · additive · 10 copies · chains A, B, C, D
- DIO · 1,4-diethylene dioxide · additive · 4 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 A0A074MDU6
- Elsewhere: RCSB PDB 7CIH · PDBe 7CIH · UniProt A0A074MDU6
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