Research workbench
Polyethylene terephthalate hydrolyzing lipase PET2 mutant - R47C-G89C- F105R-E110K-S156P-G180A-T297P
Analyse Polyethylene terephthalate hydrolyzing lipase PET2 mutant - R47C-G89C… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ECB
- Type
- protein
- Length
- 265 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- C3RYL0
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 265 | — | C3RYL0 |
Compared structures
- 7ECB · Polyethylene terephthalate hydrolyzing lipase PET2 mutant… · 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 C3RYL0
- Elsewhere: RCSB PDB 7ECB · PDBe 7ECB · UniProt C3RYL0
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