Research workbench
Crystallographic and enzymatic investigations on the role of SER558, HIS610 and ASN614 in the catalytic mechanism of azotobacter vinelandii dihydrolipoamide acetyltransferase (E2P)
Analyse Crystallographic and enzymatic investigations on the role of SER558, HIS610 and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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
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