MolNFT v1 · #4479 · protein
Crystallographic and enzymatic investigations on the role of SER558, HIS610 and ASN614 in the catalytic mechanism of azotobacter vinelandii dihydrolipoamide acetyltransferase (E2P)
1DPC: “Crystallographic and enzymatic investigations on the role of SER558, HIS610 and ASN614 in the catalytic…”. X-ray diffraction. MolNFT v1 #4479 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1DPC
- Type
- protein
- Length
- 243 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P10802
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 243 | — | P10802 |
Compared structures
- 1DPC · Crystallographic and enzymatic investigations on the role of SER558, HIS610 and ASN614 in… · the same entry in another collection · 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 P10802
- Elsewhere: RCSB PDB 1DPC · PDBe 1DPC · UniProt P10802
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.