MolNFT v1 · #4478 · protein
Crystallographic and enzymatic investigations on the role of SER558, HIS610 and ASN614 in the catalytic mechanism of azotobacter vinelandii dihydrolipoamide acetyltransferase (E2P)
1DPB: “Crystallographic and enzymatic investigations on the role of SER558, HIS610 and ASN614 in the catalytic…”. X-ray diffraction. MolNFT v1 #4478 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1DPB
- 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
- 1DPB · 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
- P10802 · AlphaFold monomer V2.0 prediction for dihydrolipoyllysine-residue acetyltransferase… · 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 P10802
- Elsewhere: RCSB PDB 1DPB · PDBe 1DPB · UniProt P10802
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