MolNFT v1 · #66652 · protein
Crystal structure and computational analyses provide insights into the catalytic mechanism of 2, 4-diacetylphloroglucinol hydrolase phlg from pseudomonas fluorescens
3HWP: “Crystal structure and computational analyses provide insights into the catalytic mechanism of 2…”. X-ray diffraction. MolNFT v1 #66652 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3HWP
- Type
- protein
- Length
- 576 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q4K423
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 288 | — | Q4K423 |
Compared structures
- 3HWP · Crystal structure and computational analyses provide insights into the catalytic… · the same entry in another collection · chain A against A, TM-score 1.00
- Q4K423 · AlphaFold monomer V2.0 prediction for 2,4-diacetylphloroglucinol hydrolase (Q4K423) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q4K423
- Elsewhere: RCSB PDB 3HWP · PDBe 3HWP · UniProt Q4K423
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