Research workbench
Structure of tev conjugated A2ML1 (A2ML1-tc)
Analyse Structure of tev conjugated A2ML1 (A2ML1-tc) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q61
- Type
- protein
- Length
- 1,210 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-2-macroglobulin-like protein 1
- UniProt
- A8K2U0
- Ligands
- NAG
- Pockets
- 18 · best druggability 0.72
Structure
electron microscopy · 1 distinct chain · 13% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-2-macroglobulin-like protein 1 | protein | 1210 | 13% helix, 42% strand | A8K2U0 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 695 | 0.72 | 0.78 | 68 | empty |
| 2 | 301 | 0.70 | 0.84 | 44 | empty |
| 3 | 146 | 0.61 | 0.84 | 23 | empty |
| 4 | 92 | 0.59 | 0.87 | 17 | empty |
| 5 | 156 | 0.50 | 0.78 | 25 | empty |
Modifications
Observed in the structure: 10 disulfide, 5 glycan (disulfide, N-glycosylation).
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 A8K2U0
- Elsewhere: RCSB PDB 7Q61 · PDBe 7Q61 · UniProt A8K2U0
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