MolNFT v1 · #4637 · protein
The structural origins of interfacial activation in thermomyces (humicola) lanuginosa lipase other structure details
1DU4: “The structural origins of interfacial activation in thermomyces (humicola) lanuginosa lipase other structure…”. X-ray diffraction. MolNFT v1 #4637 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1DU4
- Type
- protein
- Length
- 1,076 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O59952
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 269 | — | O59952 |
Compared structures
- 1DU4 · The structural origins of interfacial activation in thermomyces (humicola) lanuginosa… · the same entry in another collection · chain A against A, TM-score 1.00
- O59952 · AlphaFold monomer V2.0 prediction for lipase (O59952) · 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 O59952
- Elsewhere: RCSB PDB 1DU4 · PDBe 1DU4 · UniProt O59952
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