Research workbench
Crystal structure of a novel pet hydrolase R103G/S131A mutant in complex with hemt from ideonella sakaiensis 201-F6
Analyse Crystal structure of a novel pet hydrolase R103G/S131A mutant in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XH3
- Type
- protein
- Length
- 261 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
- 856, SO4
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | POLY(ETHYLENE terephthalate) hydrolase (EC 3.1.1.101) | protein | 261 | 30% helix, 22% strand | A0A0K8P6T7 |
Ligands and binding sites
- 856 · O 4-(2-hydroxyethyl) O 1-methyl benzene-1,4-dicarboxylate · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · chains A
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
- 5XH3 · Crystal structure of a novel PET hydrolase R103G/S131A mutant in complex with HEMT from… · 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 5XH3 · PDBe 5XH3 · UniProt A0A0K8P6T7
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