MolNFT v1 · #49063 · protein
1.0 a structure of cusf-AG(I) residues 10-88 from escherichia COLI
2QCP · Cation efflux system protein cusf: “1.0 a structure of cusf-AG(I) residues 10-88 from escherichia COLI”. X-ray diffraction, 3 ligands (AG, NO3, SO4). MolNFT v1 #49063 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2QCP
- Type
- protein
- Length
- 80 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cation efflux system protein cusf
- UniProt
- P77214
- Ligands
- AG, NO3, SO4
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Cation efflux system protein cusf | protein | 80 | 4% helix, 56% strand | P77214 |
Ligands and binding sites
- AG · Silver ion · metal · chains X
- NO3 · Nitrate ion · ion · 2 copies · chains X
- SO4 · Sulfate ion · ion · 2 copies · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2QCP · 1.0 A Structure of CusF-Ag(I) residues 10-88 from Escherichia coli · the same entry in another collection · chain X against X, TM-score 1.00
- P77214 · AlphaFold monomer V2.0 prediction for cation efflux system protein cusf (P77214) · a predicted model of the same protein · chain X against A, TM-score 0.96
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 P77214
- Elsewhere: RCSB PDB 2QCP · PDBe 2QCP · UniProt P77214
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