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Structural basis of a rationally rewired protein-protein interface (HK853MUTANT A268V, A271G, T275M, V294T and D297E)

Analyse Structural basis of a rationally rewired protein-protein interface (HK853MUTANT… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4JAU
Type: protein
Length: 232 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histidine kinase
EC: 2.7.13.3
UniProt: Q9WZV7
Ligands: ADP
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histidine kinase (EC 2.7.13.3)	protein	232	53% helix, 20% strand	Q9WZV7

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	376	0.67	0.80	50	ADP
2	101	0.37	0.75	18	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4JAU · Structural basis of a rationally rewired protein-protein interface (HK853mutant A268V… · 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 Q9WZV7
Elsewhere: RCSB PDB 4JAU · PDBe 4JAU · UniProt Q9WZV7

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