Research workbench
Structure of cagd from H. pylori pathogenicity island crystallized in the presence of CU(II) ions
Analyse Structure of cagd from H. pylori pathogenicity island crystallized in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CWY
- Type
- protein
- Length
- 130 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein cagd
- UniProt
- P94837
- Ligands
- CU
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein cagd | protein | 130 | 33% helix, 24% strand | P94837 |
Ligands and binding sites
- CU · Copper (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 modified, 1 disulfide (engineered, disulfide).
Compared structures
- 3CWY · Structure of CagD from H. pylori pathogenicity island crystallized in the presence of… · 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 P94837
- Elsewhere: RCSB PDB 3CWY · PDBe 3CWY · UniProt P94837
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