Research workbench
Cryo-EM structure of native human A2ML1
Analyse Cryo-EM structure of native human A2ML1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q5Z
- Type
- protein
- Length
- 1,344 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-2-macroglobulin-like protein 1
- UniProt
- A8K2U0
- Pockets
- 20 · best druggability 0.71
Structure
electron microscopy · 1 distinct chain · 14% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-2-macroglobulin-like protein 1 | protein | 1344 | 14% helix, 37% strand | A8K2U0 |
Pockets
20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.71 | 0.97 | 20 | empty |
| 2 | 773 | 0.69 | 0.76 | 68 | empty |
| 3 | 228 | 0.67 | 0.85 | 28 | empty |
| 4 | 320 | 0.64 | 0.80 | 40 | empty |
| 5 | 101 | 0.49 | 0.81 | 24 | empty |
Modifications
Observed in the structure: 11 disulfide (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 A8K2U0
- Elsewhere: RCSB PDB 7Q5Z · PDBe 7Q5Z · UniProt A8K2U0
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