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Catalytic domain of pknb kinase from mycobacterium tuberculosis

Analyse Catalytic domain of pknb kinase from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1O6Y
Type: protein
Length: 260 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein kinase pknb
EC: 2.7.11.1
UniProt: P0A5S4
Ligands: ACP, MG
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein kinase pknb (EC 2.7.11.1)	protein	260	40% helix, 22% strand	P0A5S4

Ligands and binding sites

ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A

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	274	0.64	0.81	37	ACP, MG

Compared structures

1O6Y · Catalytic domain of PknB kinase from Mycobacterium tuberculosis · 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 P0A5S4
Elsewhere: RCSB PDB 1O6Y · PDBe 1O6Y · UniProt P0A5S4

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