Research workbench
Understanding bi-specificity of a-domains
Analyse Understanding bi-specificity of a-domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4D56
- Type
- protein
- Length
- 482 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- APNAA1
- UniProt
- G0WVH3
- Ligands
- TYR, AMP, PO4
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | APNAA1 | protein | 482 | 32% helix, 27% strand | G0WVH3 |
Ligands and binding sites
- TYR · Tyrosine · ligand · chains A
- AMP · Adenosine monophosphate · ligand · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 757 | 0.79 | 0.83 | 96 | TYR, PO4, AMP |
| 2 | 78 | 0.39 | 0.78 | 26 | empty |
Compared structures
- 4D56 · Understanding bi-specificity of A-domains · 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 G0WVH3
- Elsewhere: RCSB PDB 4D56 · PDBe 4D56 · UniProt G0WVH3
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