Research workbench
Copm in the ag-bound form (by co-crystallization)
Analyse Copm in the ag-bound form (by co-crystallization) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FFD
- Type
- protein
- Length
- 137 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copm
- UniProt
- A0A0F6QDN6
- Ligands
- AG
Structure
x-ray diffraction · 1 distinct chain · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copm | protein | 137 | 84% helix, 0% strand | A0A0F6QDN6 |
Ligands and binding sites
- AG · Silver ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5FFD · CopM in the Ag-bound form (by co-crystallization) · 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 A0A0F6QDN6
- Elsewhere: RCSB PDB 5FFD · PDBe 5FFD · UniProt A0A0F6QDN6
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