Research workbench
Enzymatic and structural characterization of the poly (ethylene terephthalate) hydrolase petase from I. sakaiensis
Analyse Enzymatic and structural characterization of the poly (ethylene terephthalate)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YFE
- Type
- protein
- Length
- 268 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- POLY(ETHYLENE terephthalate) hydrolase
- EC
- 3.1.1.101
- UniProt
- A0A0K8P6T7
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | POLY(ETHYLENE terephthalate) hydrolase (EC 3.1.1.101) | protein | 268 | 28% helix, 22% strand | A0A0K8P6T7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5YFE · Enzymatic and structural characterization of the poly (ethylene terephthalate) hydrolase… · 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 A0A0K8P6T7
- Elsewhere: RCSB PDB 5YFE · PDBe 5YFE · UniProt A0A0K8P6T7
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