MolNFT v1 · #88294 · protein
The reaction mechanism of the N-isopropylammelide isopropylaminohydrolase atzc: insights from structural and mutagenesis studies
4CQD: “The reaction mechanism of the N-isopropylammelide isopropylaminohydrolase atzc: insights from structural and…”. X-ray diffraction. MolNFT v1 #88294 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4CQD
- Type
- protein
- Length
- 803 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O52063
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 401 | — | O52063 |
| B | — | protein | 402 | — | O52063 |
Compared structures
- 4CQD · The reaction mechanism of the N-isopropylammelide isopropylaminohydrolase AtzC: insights… · the same entry in another collection · chain A against A, TM-score 1.00
- O52063 · AlphaFold monomer V2.0 prediction for N-isopropylammelide isopropyl amidohydrolase… · a predicted model of the same protein · chain B 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 O52063
- Elsewhere: RCSB PDB 4CQD · PDBe 4CQD · UniProt O52063
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