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Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from thermobifida fusca
Analyse Structural and functional studies on a thermostable polyethylene terephthalate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CG2
- Type
- protein
- Length
- 261 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cutinase
- EC
- 3.1.1.74
- UniProt
- E5BBQ3
- Ligands
- PMS, SO4
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cutinase (EC 3.1.1.74) | protein | 261 | 31% helix, 22% strand | E5BBQ3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).
Compared structures
- 4CG2 · Structural and functional studies on a thermostable polyethylene terephthalate degrading… · 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 E5BBQ3
- Elsewhere: RCSB PDB 4CG2 · PDBe 4CG2 · UniProt E5BBQ3
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