Research workbench
The crystal structure of leaf-branch compost cutinase from biortus.
Analyse The crystal structure of leaf-branch compost cutinase from biortus. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DS7
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leaf-branch compost cutinase
- EC
- 3.1.1.74, 3.1.1.101
- UniProt
- G9BY57
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leaf-branch compost cutinase (EC 3.1.1.74, 3.1.1.101) | protein | 258 | 34% helix, 23% strand | G9BY57 |
Ligands and binding sites
- IMD · Imidazole · additive · chains A
- GOL · Glycerol · additive · chains A
- CIT · Citric acid · 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
- 7DS7 · The Crystal Structure of Leaf-branch compost cutinase from Biortus. · the same entry in another collection · chain A against A, TM-score 1.00
- G9BY57 · AlphaFold monomer V2.0 prediction for leaf-branch compost cutinase (G9BY57) · a predicted model of the same protein · 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 G9BY57
- Elsewhere: RCSB PDB 7DS7 · PDBe 7DS7 · UniProt G9BY57
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