Research workbench
Crystal Structure of the R391A Mutant of 7,8-Diaminopelargonic Acid Synthase
Analyse Crystal Structure of the R391A Mutant of 7,8-Diaminopelargonic Acid Synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MGV
- Type
- protein
- Length
- 856 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Escherichia coli
- Molecule
- 7,8-diamino-pelargonic acid aminotransferase
- EC
- 2.6.1.62
- UniProt
- P12995
- Ligands
- PLP, NA
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · resolution 2.1 · 1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 7,8-diamino-pelargonic acid aminotransferase (EC 2.6.1.62) | protein | 428 | 39% helix, 19% strand | P12995 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
- IPA · Isopropyl alcohol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 654 | 0.78 | 0.83 | 81 | PLP, IPA |
| 2 | 639 | 0.78 | 0.83 | 75 | PLP, IPA |
Interfaces
1 interface between chains.
- A–B · 5159 Ų buried · 73 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 1MGV · Crystal structure of the R391A mutant of 7,8-diaminopelargonic acid synthase · the same entry in another collection · chain A against A, TM-score 1.00
- P12995 · AlphaFold monomer V2.0 prediction for adenosylmethionine-8-amino-7-oxononanoate… · a predicted model of the same protein · 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 P12995
- Elsewhere: RCSB PDB 1MGV · PDBe 1MGV · UniProt P12995
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