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Catalytic domain of histidine kinase thka (TM1359) (nucleotide free form 4: isopropanol, orthorombic)

Analyse Catalytic domain of histidine kinase thka (TM1359) (nucleotide free form 4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3A0Z
Type: protein
Length: 293 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sensor protein
EC: 2.7.13.3
UniProt: Q9X180
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sensor protein (EC 2.7.13.3)	protein	147	39% helix, 33% strand	Q9X180
B	Sensor protein (EC 2.7.13.3)	protein	146	38% helix, 33% strand	Q9X180

Pockets

4 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	475	0.69	0.80	51	empty
2	97	0.43	0.78	19	empty
3	139	0.42	0.75	27	empty
4	51	0.27	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 656 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

3A0Z · Catalytic domain of histidine kinase ThkA (TM1359) (nucleotide free form 4: isopropanol… · 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 Q9X180
Elsewhere: RCSB PDB 3A0Z · PDBe 3A0Z · UniProt Q9X180

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