MolNFT v1 · #103827 · protein
Structure of cutinase from trichoderma reesei in its native form.
4PSC · Carbohydrate esterase family 5: “Structure of cutinase from trichoderma reesei in its native form.”. X-ray diffraction. MolNFT v1 #103827 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4PSC
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbohydrate esterase family 5
- UniProt
- G0RH85
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbohydrate esterase family 5 | protein | 220 | 49% helix, 15% strand | G0RH85 |
Ligands and binding sites
- 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: 3 disulfide (disulfide).
Compared structures
- 4PSC · Structure of cutinase from Trichoderma reesei in its native form. · 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 G0RH85
- Elsewhere: RCSB PDB 4PSC · PDBe 4PSC · UniProt G0RH85
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