Research workbench
The crystal structure of hotpetase, an evolved thermostable variant of ispetase
Analyse The crystal structure of hotpetase, an evolved thermostable variant of ispetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7QVH
- Type
- protein
- Length
- 804 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0K8P6T7
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 265 | — | A0A0K8P6T7 |
| B | — | protein | 272 | — | A0A0K8P6T7 |
| C | — | protein | 267 | — | A0A0K8P6T7 |
Ligands and binding sites
- PGE · Triethylene glycol · additive · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7QVH · The crystal structure of HotPETase, an evolved thermostable variant of IsPETase · the same entry in another collection · chain C against C, 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 7QVH · PDBe 7QVH · UniProt A0A0K8P6T7
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