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Crystal structure of the improved variant of the evolved serine hydrolase, OSH55.4_H1.2, bond with sulfate ion in the active site, northeast structural genomics consortium (nesg) target OR301
Analyse Crystal structure of the improved variant of the evolved serine hydrolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4J4Z
- Type
- protein
- Length
- 161 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Designed serine hydrolase variant OSH55.4_H1.2
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Designed serine hydrolase variant OSH55.4_H1.2 | protein | 161 | 40% helix, 22% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (engineered).
Compared structures
- 4J4Z · Crystal structure of the improved variant of the evolved serine hydrolase, OSH55.4_H1.2… · 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
- Elsewhere: RCSB PDB 4J4Z · PDBe 4J4Z
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