MolNFT v1 · #95929 · protein
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
4J4Z · Designed serine hydrolase variant OSH55.4_H1.2: “Crystal structure of the improved variant of the evolved serine hydrolase, OSH55.4_H1.2, bond with sulfate…”. X-ray diffraction, 1 ligand (SO4). MolNFT v1 #95929 on GenesisL1: 3D…
- 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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