Research workbench
Mutant R157A of fe-type nitrile hydratase from comamonas testosteroni NI1
Analyse Mutant R157A of fe-type nitrile hydratase from comamonas testosteroni NI1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZGD
- Type
- protein
- Length
- 3,296 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- J9PBS0, J9PBS1
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K, M, O | — | protein | 206 | — | J9PBS0 |
| B, D, F, H, J, L, N, P | — | protein | 206 | — | J9PBS1 |
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 J9PBS0
- Every structure of UniProt J9PBS1
- Elsewhere: RCSB PDB 4ZGD · PDBe 4ZGD · UniProt J9PBS0 · UniProt J9PBS1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.