MolNFT v1 · #117736 · protein
Indirect contributions of mutations underlie optimization of new enzyme function
5EH9: “Indirect contributions of mutations underlie optimization of new enzyme function”. X-ray diffraction. MolNFT v1 #117736 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5EH9
- Type
- protein
- Length
- 253 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0CJ63
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 253 | — | P0CJ63 |
Compared structures
- 5EH9 · Indirect contributions of mutations underlie optimization of new enzyme function · the same entry in another collection · chain A against A, TM-score 1.00
- P0CJ63 · AlphaFold monomer V2.0 prediction for N-acyl homoserine lactonase aiia (P0CJ63) · 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 P0CJ63
- Elsewhere: RCSB PDB 5EH9 · PDBe 5EH9 · UniProt P0CJ63
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