Research workbench
CU(I)-CSP3 (copper storage protein 3) from methylosinus
Analyse CU(I)-CSP3 (copper storage protein 3) from methylosinus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NQO
- Type
- protein
- Length
- 126 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CSP3
- UniProt
- A0A1I9GEP2
- Ligands
- CU1, NA
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CSP3 | protein | 126 | 79% helix, 0% strand | A0A1I9GEP2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NQO · CU(I)-CSP3 (copper storage protein 3) from methylosinus · 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 A0A1I9GEP2
- Elsewhere: RCSB PDB 5NQO · PDBe 5NQO · UniProt A0A1I9GEP2
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