Research workbench
High resolution crystal structure of a leaf-branch compost cutinase quintuple variant
Analyse High resolution crystal structure of a leaf-branch compost cutinase quintuple… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6THT
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lcc
- EC
- 3.1.1.74
- UniProt
- G9BY57
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lcc (EC 3.1.1.74) | 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
- 6THT · High resolution crystal structure of a Leaf-branch compost cutinase quintuple variant · 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 6THT · PDBe 6THT · UniProt G9BY57
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