Research workbench
Crystal structure of escherichia COLI mazg, the regulator of nutritional stress response
Analyse Crystal structure of escherichia COLI mazg, the regulator of nutritional stress… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CRC
- Type
- protein
- Length
- 445 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein mazg
- UniProt
- P0AEY3
- Ligands
- ATP, MG
- Pockets
- 7 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein mazg | protein | 225 | 69% helix, 0% strand | P0AEY3 |
| B | Protein mazg | protein | 220 | 69% helix, 0% strand | P0AEY3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 289 | 0.68 | 0.83 | 27 | empty |
| 2 | 213 | 0.67 | 0.85 | 27 | ATP |
| 3 | 222 | 0.59 | 0.80 | 35 | empty |
| 4 | 273 | 0.53 | 0.75 | 27 | empty |
| 5 | 114 | 0.52 | 0.81 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 5688 Ų buried · 48 hydrogen bonds · protein-protein
Compared structures
- 3CRC · Crystal Structure of Escherichia coli MazG, the Regulator of Nutritional Stress Response · the same entry in another collection · chain A against A, TM-score 1.00
- P0AEY3 · AlphaFold monomer V2.0 prediction for nucleoside triphosphate pyrophosphohydrolase… · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P0AEY3
- Elsewhere: RCSB PDB 3CRC · PDBe 3CRC · UniProt P0AEY3
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