Research workbench
Structure of wild-type E. COLI aspartate transcarbamoylase in the presence of CTP at 2.20 a resolution
Analyse Structure of wild-type E. COLI aspartate transcarbamoylase in the presence of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZA1
- Type
- protein
- Length
- 924 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00479, P00478
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 310 | — | P00479 |
| B, D | — | protein | 152 | — | P00478 |
Compared structures
- 1ZA1 · Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP at 2.20… · the same entry in another collection · chain D against D, 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 P00479
- Every structure of UniProt P00478
- Elsewhere: RCSB PDB 1ZA1 · PDBe 1ZA1 · UniProt P00479 · UniProt P00478
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