Research workbench
Structure of EF1P2_MFAP2B bound to dfhbi
Analyse Structure of EF1P2_MFAP2B bound to dfhbi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OHH
- Type
- protein
- Length
- 254 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- EF1P2_MFAP2B
- Ligands
- 38E, CA
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 61% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | EF1P2_MFAP2B | protein | 126 | 10% helix, 60% strand | — |
| B | EF1P2_MFAP2B | protein | 128 | 10% helix, 61% strand | — |
Ligands and binding sites
- 38E · (5Z)-5-(3,5-difluoro-4-hydroxybenzylidene)-2,3-dimethyl-3,5-dihydro-4H-imidazol-4-one · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.76 | 0.99 | 25 | 38E |
| 2 | 74 | 0.75 | 0.98 | 23 | 38E |
Interfaces
1 interface between chains.
- A–B · 711 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6OHH · Structure of EF1p2_mFAP2b bound to DFHBI · 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
- Elsewhere: RCSB PDB 6OHH · PDBe 6OHH
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