MolNFT v1 · #22530 · protein
Zn-alpha-2-glycoprotein; baculo-zag peg 200, no glycerol
1T7Y · Zinc-alpha-2-glycoprotein: “Zn-alpha-2-glycoprotein; baculo-zag peg 200, no glycerol”. X-ray diffraction, 1 ligand (NAG), 2 pockets (best druggability 0.58). MolNFT v1 #22530 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1T7Y
- Type
- protein
- Length
- 273 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Zinc-alpha-2-glycoprotein
- UniProt
- P25311
- Ligands
- NAG
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc-alpha-2-glycoprotein | protein | 273 | 26% helix, 41% strand | P25311 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · 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 | 230 | 0.58 | 0.79 | 20 | empty |
| 2 | 51 | 0.30 | 0.76 | 14 | empty |
Modifications
Observed in the structure: 2 glycan, 1 disulfide (N-glycosylation, disulfide).
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 P25311
- Elsewhere: RCSB PDB 1T7Y · PDBe 1T7Y · UniProt P25311
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