Research workbench
Crystal structure of adzuki bean 7S globulin-3
Analyse Crystal structure of adzuki bean 7S globulin-3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EAA
- Type
- protein
- Length
- 1,132 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 7S globulin-3
- UniProt
- A4PIA0
- Ligands
- CA
- Pockets
- 8 · best druggability 0.70
Structure
x-ray diffraction · 3 distinct chains · 19% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 7S globulin-3 | protein | 375 | 20% helix, 43% strand | A4PIA0 |
| B | 7S globulin-3 | protein | 380 | 18% helix, 42% strand | A4PIA0 |
| C | 7S globulin-3 | protein | 377 | 20% helix, 42% strand | A4PIA0 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A, C, B
- CIT · Citric acid · additive · 3 copies · chains A, B, C
- ACY · Acetic acid · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1142 | 0.70 | 0.74 | 116 | empty |
| 2 | 304 | 0.62 | 0.79 | 36 | empty |
| 3 | 270 | 0.59 | 0.78 | 28 | empty |
| 4 | 260 | 0.58 | 0.78 | 32 | empty |
| 5 | 86 | 0.35 | 0.75 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–C · 2751 Ų buried · 34 hydrogen bonds · protein-protein
- B–C · 2732 Ų buried · 34 hydrogen bonds · protein-protein
- A–B · 2694 Ų buried · 35 hydrogen bonds · protein-protein
Compared structures
- 2EAA · Crystal Structure of Adzuki Bean 7S Globulin-3 · the same entry in another collection · chain A against A, TM-score 1.00
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 A4PIA0
- Elsewhere: RCSB PDB 2EAA · PDBe 2EAA · UniProt A4PIA0
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