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Crystal structure of the DNA binding domain of cpxr from E. COLI

Analyse Crystal structure of the DNA binding domain of cpxr from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4UHT
Type: protein
Length: 204 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcriptional regulatory protein cpxr
UniProt: P0AE88
Ligands: CL
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transcriptional regulatory protein cpxr	protein	102	32% helix, 22% strand	P0AE88

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	68	0.37	0.78	17	empty

Interfaces

1 interface between chains.

A–B · 447 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

4UHT · Crystal structure of the DNA binding domain of CpxR from E. coli · the same entry in another collection · chain A against A, TM-score 1.00
P0AE88 · AlphaFold monomer V2.0 prediction for transcriptional regulatory protein cpxr (P0AE88) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 P0AE88
Elsewhere: RCSB PDB 4UHT · PDBe 4UHT · UniProt P0AE88

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