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Structure of the carboxyl transferase domain from rhizobium etli pyruvate carboxylase with pyruvate
Analyse Structure of the carboxyl transferase domain from rhizobium etli pyruvate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JX5
- Type
- protein
- Length
- 2,374 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q2K340
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 597 | — | Q2K340 |
| B | — | protein | 596 | — | Q2K340 |
| C | — | protein | 591 | — | Q2K340 |
| D | — | protein | 590 | — | Q2K340 |
Compared structures
- 4JX5 · Structure of the carboxyl transferase domain from Rhizobium etli pyruvate carboxylase… · 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 Q2K340
- Elsewhere: RCSB PDB 4JX5 · PDBe 4JX5 · UniProt Q2K340
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