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Active histidine kinase bound with ATP

Analyse Active histidine kinase bound with ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4U7O
Type: protein
Length: 452 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histidine protein kinase sensor protein
UniProt: C6VIM1
Ligands: AN2
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histidine protein kinase sensor protein	protein	234	51% helix, 21% strand	C6VIM1
B	Histidine protein kinase sensor protein	protein	218	47% helix, 22% strand	C6VIM1

Ligands and binding sites

AN2 · Amp phosphoramidate · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	238	0.76	0.90	37	AN2
2	407	0.68	0.80	45	AN2
3	128	0.49	0.79	19	empty
4	184	0.47	0.75	23	empty
5	131	0.40	0.74	24	empty

Interfaces

1 interface between chains.

A–B · 1536 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

4U7O · Active histidine kinase bound with ATP · 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 C6VIM1
Elsewhere: RCSB PDB 4U7O · PDBe 4U7O · UniProt C6VIM1

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