Research workbench
Aspartate transcarbamoylase catalytic chain mutant GLU50ALA complexed with N-(phosphonacetyl-L-aspartate) (pala)
Analyse Aspartate transcarbamoylase catalytic chain mutant GLU50ALA complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TTH
- Type
- protein
- Length
- 926 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0A786, P0A7F3
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 310 | — | P0A786 |
| B, D | — | protein | 153 | — | P0A7F3 |
Compared structures
- 1TTH · Aspartate Transcarbamoylase Catalytic Chain Mutant Glu50Ala Complexed with… · 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 P0A786
- Every structure of UniProt P0A7F3
- Elsewhere: RCSB PDB 1TTH · PDBe 1TTH · UniProt P0A786 · UniProt P0A7F3
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