Research workbench
E. COLI atcase holoenzyme mutant - G128/130A (catalytic chain)
Analyse E. COLI atcase holoenzyme mutant - G128/130A (catalytic chain) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KJA
- Type
- protein
- Length
- 1,311 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0A786, P0A7F3
- Ligands
- ZN
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 303 | — | P0A786 |
| B, F | — | protein | 134 | — | P0A7F3 |
| C | — | protein | 303 | — | P0A786 |
| D | — | protein | 133 | — | P0A7F3 |
| E | — | protein | 304 | — | P0A786 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains B, D, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6KJA · E. coli ATCase holoenzyme mutant - G128/130A (catalytic chain) · 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 6KJA · PDBe 6KJA · UniProt P0A786 · UniProt P0A7F3
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