MolNFT v1 · #176908 · protein
Structure of MREB3 from spiroplasma eriocheiris
7E1G · Cell shape-determining protein mreb: “Structure of MREB3 from spiroplasma eriocheiris”. X-ray diffraction, 2 ligands (ANP, MG), 6 pockets (best druggability 0.74). MolNFT v1 #176908 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7E1G
- Type
- protein
- Length
- 662 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell shape-determining protein mreb
- UniProt
- A0A0H3XJK5
- Ligands
- ANP, MG
- Pockets
- 6 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell shape-determining protein mreb | protein | 332 | 40% helix, 28% strand | A0A0H3XJK5 |
| B | Cell shape-determining protein mreb | protein | 330 | 39% helix, 28% strand | A0A0H3XJK5 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 467 | 0.74 | 0.83 | 58 | MG, ANP |
| 2 | 458 | 0.72 | 0.82 | 58 | MG, ANP |
| 3 | 420 | 0.58 | 0.74 | 38 | empty |
| 4 | 84 | 0.41 | 0.78 | 15 | empty |
| 5 | 70 | 0.38 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 230 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 42 modified, 1 covalent (methylation, covalent ligand).
Compared structures
- 7E1G · Structure of MreB3 from Spiroplasma eriocheiris · 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 A0A0H3XJK5
- Elsewhere: RCSB PDB 7E1G · PDBe 7E1G · UniProt A0A0H3XJK5
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