Research workbench
Crystal structure of the nematode sperm cell motility protein MFP2B
Analyse Crystal structure of the nematode sperm cell motility protein MFP2B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BJR
- Type
- protein
- Length
- 720 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MFP2B
- UniProt
- Q7YXJ9
- Ligands
- ZN, SO4
- Pockets
- 11 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MFP2B | protein | 363 | 11% helix, 48% strand | Q7YXJ9 |
| B | MFP2B | protein | 357 | 11% helix, 48% strand | Q7YXJ9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1190 | 0.74 | 0.77 | 76 | empty |
| 2 | 1093 | 0.73 | 0.76 | 68 | empty |
| 3 | 361 | 0.68 | 0.81 | 48 | empty |
| 4 | 74 | 0.47 | 0.82 | 15 | empty |
| 5 | 149 | 0.46 | 0.77 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 459 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 modified (engineered).
Compared structures
- 2BJR · Crystal structure of the nematode sperm cell motility protein MFP2B · 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 Q7YXJ9
- Elsewhere: RCSB PDB 2BJR · PDBe 2BJR · UniProt Q7YXJ9
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