Research workbench
Crystal structure of E. COLI phosphoenolpyruvate carboxykinase mutant LYS254SER
Analyse Crystal structure of E. COLI phosphoenolpyruvate carboxykinase mutant LYS254SER in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V2N
- Type
- protein
- Length
- 518 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoenolpyruvate carboxykinase (ATP)
- EC
- 4.1.1.49
- UniProt
- A0A400L9R1
- Ligands
- CA
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoenolpyruvate carboxykinase (ATP) (EC 4.1.1.49) | protein | 518 | 30% helix, 25% strand | A0A400L9R1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 587 | 0.66 | 0.77 | 62 | CA, ACT |
| 2 | 88 | 0.37 | 0.76 | 20 | empty |
Compared structures
- 6V2N · Crystal structure of E. coli phosphoenolpyruvate carboxykinase mutant Lys254Ser · 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 A0A400L9R1
- Elsewhere: RCSB PDB 6V2N · PDBe 6V2N · UniProt A0A400L9R1
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