MolNFT v1 · #7235 · protein
The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (rmla). THYMIDINE/GLUCOSE- 1-phosphate complex.
1G0R: “The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase…”. X-ray diffraction. MolNFT v1 #7235 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1G0R
- Type
- protein
- Length
- 2,337 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9HU22
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, G, H | — | protein | 292 | — | Q9HU22 |
| F | — | protein | 293 | — | Q9HU22 |
Compared structures
- 1G0R · The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… · 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 Q9HU22
- Elsewhere: RCSB PDB 1G0R · PDBe 1G0R · UniProt Q9HU22
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