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Escherichia COLI glutamine phosphoribosylpyrophosphate (prpp) amidotransferase complexed with 2 AMP per tetramer
Analyse Escherichia COLI glutamine phosphoribosylpyrophosphate (prpp) amidotransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ECJ
- Type
- protein
- Length
- 1,968 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00496
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 492 | — | P00496 |
Compared structures
- 1ECJ · Escherichia COLI glutamine phosphoribosylpyrophosphate (prpp) amidotransferase complexed… · 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 P00496
- Elsewhere: RCSB PDB 1ECJ · PDBe 1ECJ · UniProt P00496
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