MolNFT v1 · #175049 · protein
Crystal structure of pet-degrading cutinase CUT190 S176A/S226P/R228S/ mutant with the C-terminal three residues deletion in ligand ejecting form
7CEH · ALPHA/BETA hydrolase family protein: “Crystal structure of pet-degrading cutinase CUT190 S176A/S226P/R228S/ mutant with the C-terminal three…”. X-ray diffraction, 1 ligand (CA). MolNFT v1 #175049 on GenesisL1: 3D structure, binding…
- PDB
- 7CEH
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- 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
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ALPHA/BETA hydrolase family protein (EC 3.1.1.74) | protein | 259 | 31% helix, 22% strand | W0TJ64 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7CEH · Crystal structure of PET-degrading cutinase Cut190 S176A/S226P/R228S/ mutant with the… · 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 7CEH · PDBe 7CEH · UniProt W0TJ64
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