Research workbench
Crystal structure of tarin lectin bound to trimannose
Analyse Crystal structure of tarin lectin bound to trimannose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5T20
- Type
- protein
- Length
- 1,738 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A5HMM7
- Ligands
- MAN
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, G, I, K, M, O | — | protein | 108 | — | A5HMM7 |
| B, D, F, H, J, L, N, P | — | protein | 109 | — | — |
| C, E | — | protein | 109 | — | A5HMM7 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 48 copies · chains A, J, I, B, C, N, M, D, F, E, L, K, G, P, O, H
- EDO · 1,2-ethanediol · additive · 2 copies · chains J, L, G, O
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5T20 · Crystal Structure of Tarin Lectin bound to Trimannose · the same entry in another collection · chain P against P, 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 A5HMM7
- Elsewhere: RCSB PDB 5T20 · PDBe 5T20 · UniProt A5HMM7
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