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Crystal structure of the extracellular domain of the putative histidine kinase MMHK1S-Z2

Analyse Crystal structure of the extracellular domain of the putative histidine kinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LI8
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical sensory transduction histidine kinase
UniProt: Q8PSW8
Ligands: SO4
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical sensory transduction histidine kinase	protein	263	34% helix, 29% strand	Q8PSW8

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 4 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	74	0.43	0.80	16	EDO, SO4
2	130	0.43	0.75	24	empty

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

3LI8 · Crystal Structure of the extracellular domain of the putative histidine kinase mmHK1S-Z2 · 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 Q8PSW8
Elsewhere: RCSB PDB 3LI8 · PDBe 3LI8 · UniProt Q8PSW8

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