Research workbench
Cryo-EM structure of "CT react" conformation of Lactococcus lactis pyruvate carboxylase with acetyl-CoA
Analyse Cryo-EM structure of "CT react" conformation of Lactococcus lactis pyruvate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ZZ1
- Type
- protein
- Length
- 618 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.27
- Source
- Lactococcus lactis
- Molecule
- Pyruvate carboxylase
- EC
- 6.4.1.1
- UniProt
- A0A2A9IR05
- Ligands
- OAA, BTN, MG, MN
- Pockets
- 4 · best druggability 0.75
Structure
electron microscopy · resolution 2.27 · 2 distinct chains · 46% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyruvate carboxylase (EC 6.4.1.1) | protein | 541 | 53% helix, 8% strand | A0A2A9IR05 |
| B | Pyruvate carboxylase (EC 6.4.1.1) | protein | 77 | 0% helix, 40% strand | A0A2A9IR05 |
Ligands and binding sites
- OAA · Oxaloacetate ion · ligand · chains A
- BTN · Biotin · ligand · chains A, B
- MG · Magnesium ion · metal · chains A
- MN · Manganese (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 737 | 0.75 | 0.80 | 91 | OAA, BTN |
| 2 | 299 | 0.68 | 0.83 | 24 | empty |
| 3 | 65 | 0.30 | 0.74 | 18 | empty |
| 4 | 76 | 0.30 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 871 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 cofactor, 1 modified (biotinylation, carboxylation).
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 A0A2A9IR05
- Elsewhere: RCSB PDB 7ZZ1 · PDBe 7ZZ1 · UniProt A0A2A9IR05
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.