MolNFT v1 · #153476 · protein
Nucleotide-free MITOFUSIN2 (MFN2)
6JFL · Mitofusin-2,CDNA FLJ57997, highly similar to transmembrane…: “Nucleotide-free MITOFUSIN2 (MFN2)”. X-ray diffraction, 1 ligand (CA), 19 pockets (best druggability 0.78). MolNFT v1 #153476 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6JFL
- Type
- protein
- Length
- 1,653 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitofusin-2,CDNA FLJ57997, highly similar to transmembrane GTPase MFN2
- EC
- 3.6.5.-
- UniProt
- O95140, B7Z3H8
- Ligands
- CA
- Pockets
- 19 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 61% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitofusin-2,CDNA FLJ57997, highly similar to transmembrane GTPase MFN2 (EC 3.6.5.-) | protein | 413 | 61% helix, 11% strand | O95140, B7Z3H8 |
| B | Mitofusin-2,CDNA FLJ57997, highly similar to transmembrane GTPase MFN2 (EC 3.6.5.-) | protein | 413 | 61% helix, 12% strand | O95140, B7Z3H8 |
| C | Mitofusin-2,CDNA FLJ57997, highly similar to transmembrane GTPase MFN2 (EC 3.6.5.-) | protein | 412 | 62% helix, 11% strand | O95140, B7Z3H8 |
| D | Mitofusin-2,CDNA FLJ57997, highly similar to transmembrane GTPase MFN2 (EC 3.6.5.-) | protein | 415 | 61% helix, 12% strand | O95140, B7Z3H8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1128 | 0.78 | 0.80 | 97 | empty |
| 2 | 568 | 0.75 | 0.82 | 63 | empty |
| 3 | 881 | 0.74 | 0.78 | 58 | empty |
| 4 | 383 | 0.67 | 0.81 | 36 | GOL |
| 5 | 511 | 0.66 | 0.78 | 40 | empty |
Interfaces
4 interfaces between chains.
- B–D · 1587 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 1472 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 359 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 313 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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 O95140
- Every structure of UniProt B7Z3H8
- Elsewhere: RCSB PDB 6JFL · PDBe 6JFL · UniProt O95140 · UniProt B7Z3H8
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