MolNFT v1 · #40517 · protein
Site directed mutagenesis of key residues involved in the catalytic mechanism of cyanase
2IV1: “Site directed mutagenesis of key residues involved in the catalytic mechanism of cyanase”. X-ray diffraction. MolNFT v1 #40517 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2IV1
- Type
- protein
- Length
- 1,560 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00816
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | — | protein | 156 | — | P00816 |
Compared structures
- 2IV1 · Site directed mutagenesis of key residues involved in the catalytic mechanism of cyanase · the same entry in another collection · chain J against J, TM-score 1.00
- P00816 · AlphaFold monomer V2.0 prediction for cyanate hydratase (P00816) · a predicted model of the same protein · chain H 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 P00816
- Elsewhere: RCSB PDB 2IV1 · PDBe 2IV1 · UniProt P00816
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