MolNFT v1 · #4357 · protein
The first structure of udp-glucose dehydrogenase (udpgdh) reveals the catalytic residues necessary for the two-fold oxidation
1DLI: “The first structure of udp-glucose dehydrogenase (udpgdh) reveals the catalytic residues necessary for the…”. X-ray diffraction. MolNFT v1 #4357 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1DLI
- Type
- protein
- Length
- 402 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0C0F4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 402 | — | P0C0F4 |
Compared structures
- 1DLI · The first structure of udp-glucose dehydrogenase (udpgdh) reveals the catalytic residues… · the same entry in another collection · chain A against A, TM-score 1.00
- P0C0F4 · AlphaFold monomer V2.0 prediction for udp-glucose 6-dehydrogenase (P0C0F4) · a predicted model of the same protein · 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 P0C0F4
- Elsewhere: RCSB PDB 1DLI · PDBe 1DLI · UniProt P0C0F4
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