Research workbench
Crystal structure determination and refinement at 2.3 ångströms resolution of the lentil lectin
Analyse Crystal structure determination and refinement at 2.3 ångströms resolution of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LAL
- Type
- protein
- Length
- 456 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02870
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 181 | — | P02870 |
| B, D | — | protein | 47 | — | P02870 |
Compared structures
- 2LAL · Crystal structure determination and refinement at 2.3 ångströms resolution of the lentil… · the same entry in another collection · chain A against A, TM-score 1.00
- P02870 · AlphaFold monomer V2.0 prediction for lectin (P02870) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P02870
- Elsewhere: RCSB PDB 2LAL · PDBe 2LAL · UniProt P02870
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