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Crystal structure of human glycosylated angiotensinogen
Analyse Crystal structure of human glycosylated angiotensinogen in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5M3Y
- Type
- protein
- Length
- 418 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Angiotensinogen
- UniProt
- P01019
- Ligands
- NAG, BMA
- Pockets
- 4 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Angiotensinogen | protein | 418 | 31% helix, 30% strand | P01019 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- BMA · beta-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.38 | 0.75 | 18 | empty |
| 2 | 58 | 0.36 | 0.79 | 16 | empty |
| 3 | 58 | 0.34 | 0.78 | 17 | empty |
| 4 | 50 | 0.31 | 0.77 | 15 | empty |
Modifications
Observed in the structure: 1 disulfide, 1 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 P01019
- Elsewhere: RCSB PDB 5M3Y · PDBe 5M3Y · UniProt P01019
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