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Closed form of pet-degrading cutinase CUT190 with thermostability- improving mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H
Analyse Closed form of pet-degrading cutinase CUT190 with thermostability- improving… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CTR
- Type
- protein
- Length
- 518 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ALPHA/BETA hydrolase family protein
- EC
- 3.1.1.74
- UniProt
- W0TJ64
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ALPHA/BETA hydrolase family protein (EC 3.1.1.74) | protein | 259 | 31% helix, 25% strand | W0TJ64 |
Ligands and binding sites
- DIO · 1,4-diethylene dioxide · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 7CTR · Closed form of PET-degrading cutinase Cut190 with thermostability-improving mutations of… · 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 W0TJ64
- Elsewhere: RCSB PDB 7CTR · PDBe 7CTR · UniProt W0TJ64
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