MolNFT v1 · #6816 · protein
Crystal structure analysis of N-carbamoyl-D-amino-acid amidohydrolase
1FO6: “Crystal structure analysis of N-carbamoyl-D-amino-acid amidohydrolase”. X-ray diffraction. MolNFT v1 #6816 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1FO6
- Type
- protein
- Length
- 1,208 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q44185
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 302 | — | Q44185 |
Compared structures
- 1FO6 · CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE · the same entry in another collection · chain D against D, TM-score 1.00
- Q44185 · AlphaFold monomer V2.0 prediction for N-carbamoyl-D-amino acid hydrolase (Q44185) · 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 Q44185
- Elsewhere: RCSB PDB 1FO6 · PDBe 1FO6 · UniProt Q44185
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