MolNFT v1 · #60427 · protein
Crystal structure of escherichia COLI mazg, the regulator of nutritional stress response
3CRC · Protein mazg: “Crystal structure of escherichia COLI mazg, the regulator of nutritional stress response”. X-ray diffraction, 2 ligands (ATP, MG), 7 pockets (best druggability 0.68). MolNFT v1 #60427 on GenesisL1: 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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