Research workbench
Haddock structure of TGMIC4-A5/LACTO-N-biose complex, based on noe- derived distance restraints
Analyse Haddock structure of TGMIC4-A5/LACTO-N-biose complex, based on noe- derived… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LL4
- Type
- protein
- Length
- 70 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Micronemal protein 4
- UniProt
- Q9XZH7
- Ligands
- NAG, GAL
Structure
solution nmr · 1 distinct chain · 14% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| M | Micronemal protein 4 | protein | 70 | 14% helix, 31% strand | Q9XZH7 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains M
- GAL · beta-D-galactopyranose · sugar · chains M
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 2LL4 · HADDOCK structure of TgMIC4-A5/lacto-N-biose complex, based on NOE-derived distance… · the same entry in another collection · chain M against M, TM-score 1.00
- Q9XZH7 · AlphaFold monomer V2.0 prediction for micronemal protein 4 (Q9XZH7) · a predicted model of the same protein · chain M against A, TM-score 0.85
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 Q9XZH7
- Elsewhere: RCSB PDB 2LL4 · PDBe 2LL4 · UniProt Q9XZH7
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