Research workbench
Crystal structure of native alpha-2-macroglobulin from escherichia COLI spanning domains MG0-nie-MG1.
Analyse Crystal structure of native alpha-2-macroglobulin from escherichia COLI… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZJG
- Type
- protein
- Length
- 304 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-2-macroglobulin
- UniProt
- P76578
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-2-macroglobulin | protein | 304 | 6% helix, 48% strand | P76578 |
Ligands and binding sites
- GOL · Glycerol · additive · 5 copies · chains A
- PG4 · Tetraethylene glycol · additive · chains A
- PGE · Triethylene glycol · additive · chains A
- 1PE · Pentaethylene glycol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.45 | 0.79 | 14 | empty |
| 2 | 66 | 0.29 | 0.73 | 19 | empty |
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 4ZJG · Crystal structure of native alpha-2-macroglobulin from Escherichia coli spanning domains… · the same entry in another collection · chain A against A, TM-score 1.00
- P76578 · AlphaFold monomer V2.0 prediction for alpha-2-macroglobulin (P76578) · a predicted model of the same protein · chain A against A, TM-score 0.76
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 P76578
- Elsewhere: RCSB PDB 4ZJG · PDBe 4ZJG · UniProt P76578
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