Research workbench
Crystal structure of human PACSIN2 F-bar domain (P212121 lattice)
Analyse Crystal structure of human PACSIN2 F-bar domain (P212121 lattice) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HAJ
- Type
- protein
- Length
- 570 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human PACSIN2 F-bar
- UniProt
- Q9UNF0
- Ligands
- CA
- Pockets
- 4 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 80% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human PACSIN2 F-bar | protein | 286 | 82% helix, 1% strand | Q9UNF0 |
| B | Human PACSIN2 F-bar | protein | 284 | 78% helix, 1% strand | Q9UNF0 |
Ligands and binding sites
- 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
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.59 | 0.87 | 19 | empty |
| 2 | 143 | 0.54 | 0.81 | 20 | empty |
| 3 | 76 | 0.37 | 0.77 | 15 | empty |
| 4 | 64 | 0.33 | 0.76 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 4235 Ų buried · 35 hydrogen bonds · protein-protein
Compared structures
- 3HAJ · Crystal structure of human PACSIN2 F-BAR domain (p212121 lattice) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UNF0 · AlphaFold monomer V2.0 prediction for protein kinase C and casein kinase substrate in… · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q9UNF0
- Elsewhere: RCSB PDB 3HAJ · PDBe 3HAJ · UniProt Q9UNF0
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