MolNFT v1 · #23404 · protein
X-ray structure of northeast structural genomics consortium target SOR45
1TZA · Apag protein: “X-ray structure of northeast structural genomics consortium target SOR45”. X-ray diffraction, 2 pockets (best druggability 0.63). MolNFT v1 #23404 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1TZA
- Type
- protein
- Length
- 261 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apag protein
- UniProt
- Q8EB92
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 1% helix, 63% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Apag protein | protein | 132 | 2% helix, 63% strand | Q8EB92 |
| B | Apag protein | protein | 129 | 0% helix, 63% strand | Q8EB92 |
Ligands and binding sites
- CAC · Cacodylate ion · additive · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 269 | 0.63 | 0.81 | 33 | empty |
| 2 | 81 | 0.42 | 0.79 | 16 | CAC |
Interfaces
1 interface between chains.
- A–B · 686 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
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 Q8EB92
- Elsewhere: RCSB PDB 1TZA · PDBe 1TZA · UniProt Q8EB92
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