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NMR structure of the histidine kinase domain of the E. COLI osmosensor envz

Analyse NMR structure of the histidine kinase domain of the E. COLI osmosensor envz in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BXD
Type: protein
Length: 161 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (osmolarity sensor protein (envz))
EC: 2.7.3.-
UniProt: P02933
Ligands: ANP
Pockets: 1 · best druggability 0.55

Structure

solution nmr · 1 distinct chain · 24% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (osmolarity sensor protein (envz)) (EC 2.7.3.-)	protein	161	24% helix, 26% strand	P02933

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	212	0.55	0.78	26	ANP

Compared structures

1BXD · NMR structure of the histidine kinase domain of the E. COLI osmosensor envz · 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 P02933
Elsewhere: RCSB PDB 1BXD · PDBe 1BXD · UniProt P02933

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