Research workbench
Crystal structure of the cpx pathway activator nlpe from escherichia COLI
Analyse Crystal structure of the cpx pathway activator nlpe from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z4I
- Type
- protein
- Length
- 384 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper homeostasis protein cutf
- UniProt
- P40710
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper homeostasis protein cutf | protein | 190 | 6% helix, 53% strand | P40710 |
| B | Copper homeostasis protein cutf | protein | 194 | 5% helix, 51% strand | P40710 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.36 | 0.75 | 17 | empty |
| 2 | 51 | 0.25 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 2074 Ų buried · 35 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified, 4 disulfide (engineered, disulfide).
Compared structures
- 2Z4I · Crystal structure of the Cpx pathway activator NlpE from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
- P40710 · AlphaFold monomer V2.0 prediction for lipoprotein nlpe (P40710) · a predicted model of the same protein · chain B against A, TM-score 0.51
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 P40710
- Elsewhere: RCSB PDB 2Z4I · PDBe 2Z4I · UniProt P40710
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