Research workbench
Structural basis for recognition of frizzled proteins by clostridium difficile toxin B
Analyse Structural basis for recognition of frizzled proteins by clostridium difficile… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C0B
- Type
- protein
- Length
- 627 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- M4NKV9, Q14332
- Ligands
- PAM, NAG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 506 | — | M4NKV9 |
| B | — | protein | 121 | — | Q14332 |
Ligands and binding sites
- PAM · Palmitoleic acid · ligand · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains B
- MLI · Malonate ion · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6C0B · Structural basis for recognition of frizzled proteins by Clostridium difficile toxin B · the same entry in another collection · chain A against A, TM-score 1.00
- Q14332 · AlphaFold monomer V2.0 prediction for frizzled-2 (Q14332) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 M4NKV9
- Every structure of UniProt Q14332
- Elsewhere: RCSB PDB 6C0B · PDBe 6C0B · UniProt M4NKV9 · UniProt Q14332
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