Research workbench
The crystal structure of a thermobifida fusca cutinase
Analyse The crystal structure of a thermobifida fusca cutinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZOA
- Type
- protein
- Length
- 261 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bta-hydrolase 1
- EC
- 3.1.1.74
- UniProt
- Q6A0I4
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bta-hydrolase 1 (EC 3.1.1.74) | protein | 261 | 31% helix, 21% strand | Q6A0I4 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5ZOA · The crystal structure of a Thermobifida fusca cutinase · 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 Q6A0I4
- Elsewhere: RCSB PDB 5ZOA · PDBe 5ZOA · UniProt Q6A0I4
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