Research workbench
Crystal structure of C-type lectin cel-I from cucumaria echinata
Analyse Crystal structure of C-type lectin cel-I from cucumaria echinata in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WMY
- Type
- protein
- Length
- 280 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lectin cel-I, N-acetyl-D-galactosamine-specific C-type
- UniProt
- Q7M462
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Lectin cel-I, N-acetyl-D-galactosamine-specific C-type | protein | 140 | 21% helix, 34% strand | Q7M462 |
Ligands and binding sites
- CA · Calcium ion · metal · 6 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 856 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 1WMY · Crystal Structure of C-type Lectin CEL-I from Cucumaria echinata · 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 Q7M462
- Elsewhere: RCSB PDB 1WMY · PDBe 1WMY · UniProt Q7M462
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