Research workbench
The pub domain functions as a P97 binding module in human peptide N- glycanase.
Analyse The pub domain functions as a P97 binding module in human peptide N- glycanase. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CCQ
- Type
- protein
- Length
- 99 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptide N-glycanase homolog
- UniProt
- Q9BVR8
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptide N-glycanase homolog | protein | 99 | 57% helix, 8% strand | Q9BVR8 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2CCQ · The PUB domain functions as a p97 binding module in human peptide N-glycanase. · 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 Q9BVR8
- Elsewhere: RCSB PDB 2CCQ · PDBe 2CCQ · UniProt Q9BVR8
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