Research workbench
Crystal structure of plant lectin from cicer arietinum at 2.6 ångström resolution
Analyse Crystal structure of plant lectin from cicer arietinum at 2.6 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OEI
- Type
- protein
- Length
- 448 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lectin
- UniProt
- G1K3R9
- Ligands
- MG, SO4
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Lectin | protein | 224 | 17% helix, 38% strand | G1K3R9 |
Ligands and binding sites
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 | 59 | 0.38 | 0.80 | 15 | empty |
| 2 | 56 | 0.38 | 0.80 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 690 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 4OEI · Crystal structure of plant lectin from Cicer arietinum at 2.6 angstrom resolution · 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 G1K3R9
- Elsewhere: RCSB PDB 4OEI · PDBe 4OEI · UniProt G1K3R9
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