Research workbench
E. coli ATCase holoenzyme mutant - G166P (catalytic chain)
Analyse E. coli ATCase holoenzyme mutant - G166P (catalytic chain) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KJ8
- Type
- protein
- Length
- 1,312 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.011
- Source
- Escherichia coli K-12
- Molecule
- Aspartate carbamoyltransferase catalytic subunit; Aspartate carbamoyltransferase…
- EC
- 2.1.3.2
- UniProt
- P0A786, P0A7F3
- Ligands
- ZN
- Pockets
- 12 · best druggability 0.82
Structure
x-ray diffraction · resolution 3.011 · 6 distinct chains · 34% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate carbamoyltransferase catalytic subunit (EC 2.1.3.2) | protein | 301 | 44% helix, 16% strand | P0A786 |
| B | Aspartate carbamoyltransferase regulatory chain | protein | 135 | 16% helix, 33% strand | P0A7F3 |
| C | Aspartate carbamoyltransferase catalytic subunit (EC 2.1.3.2) | protein | 303 | 43% helix, 16% strand | P0A786 |
| D | Aspartate carbamoyltransferase regulatory chain | protein | 129 | 12% helix, 26% strand | P0A7F3 |
| E | Aspartate carbamoyltransferase catalytic subunit (EC 2.1.3.2) | protein | 301 | 44% helix, 17% strand | P0A786 |
| F | Aspartate carbamoyltransferase regulatory chain | protein | 143 | 12% helix, 38% strand | P0A7F3 |
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.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 952 | 0.82 | 0.83 | 98 | empty |
| 2 | 412 | 0.67 | 0.80 | 47 | empty |
| 3 | 455 | 0.66 | 0.78 | 53 | empty |
| 4 | 418 | 0.64 | 0.78 | 48 | empty |
| 5 | 128 | 0.57 | 0.83 | 21 | empty |
Interfaces
9 interfaces between chains.
- C–E · 872 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 869 Ų buried · 12 hydrogen bonds · protein-protein
- A–E · 836 Ų buried · 7 hydrogen bonds · protein-protein
- E–F · 672 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 669 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 6KJ8 · E. COLI atcase holoenzyme mutant - G166P (catalytic chain) · the same entry in another collection · chain F against F, TM-score 1.00
- P0A786 · AlphaFold monomer V2.0 prediction for aspartate carbamoyltransferase catalytic subunit… · a predicted model of the same protein · chain E against A, TM-score 0.98
- P0A7F3 · AlphaFold monomer V2.0 prediction for aspartate carbamoyltransferase regulatory chain… · a predicted model of the same protein · chain B against A, TM-score 0.96
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 6KJ8 · PDBe 6KJ8 · UniProt P0A786 · UniProt P0A7F3
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