Research workbench

Crystal structure of a putative sensor histidine kinase domain from clostridium symbiosum atcc 14940

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

PDB: 3FN2
Type: protein
Length: 194 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative sensor histidine kinase domain
Ligands: K, PO4
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative sensor histidine kinase domain	protein	97	41% helix, 21% strand	—

Ligands and binding sites

K · Potassium ion · metal · chains A, B
PO4 · Phosphate ion · ion · chains B
EDO · 1,2-ethanediol · additive · chains 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	126	0.57	0.84	31	empty

Interfaces

1 interface between chains.

A–B · 3007 Å² buried · 25 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

3FN2 · Crystal structure of a putative sensor histidine kinase domain from Clostridium symbiosum… · 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
Elsewhere: RCSB PDB 3FN2 · PDBe 3FN2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.