MolNFT v1 · #102228 · protein
Crystal structure of syg-2 D4
4OFK · Protein syg-2: “Crystal structure of syg-2 D4”. X-ray diffraction, 3 ligands (NAG, CL, SO4). MolNFT v1 #102228 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4OFK
- Type
- protein
- Length
- 207 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein syg-2
- UniProt
- Q9U3P2
- Ligands
- NAG, CL, SO4
Structure
x-ray diffraction · 2 distinct chains · 1% helix, 62% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein syg-2 | protein | 103 | 0% helix, 63% strand | Q9U3P2 |
| B | Protein syg-2 | protein | 104 | 3% helix, 62% strand | Q9U3P2 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A
- SO4 · Sulfate ion · ion · chains B
- EDO · 1,2-ethanediol · 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 · 333 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
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 Q9U3P2
- Elsewhere: RCSB PDB 4OFK · PDBe 4OFK · UniProt Q9U3P2
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