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Structure of PKBalpha PH domain in complex with a novel inositol headgroup surrogate, benzene 1,2,3,4-tetrakisphosphate

Analyse Structure of PKBalpha PH domain in complex with a novel inositol headgroup… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2UVM
Type: protein
Length: 115 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.94
Source: HOMO SAPIENS
Molecule: Rac-alpha SERINE/THREONINE-protein kinase
EC: 2.7.11.1
UniProt: P31749
Ligands: GVF, NA

Structure

x-ray diffraction · resolution 1.94 · 1 distinct chain · 24% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rac-alpha SERINE/THREONINE-protein kinase (EC 2.7.11.1)	protein	115	24% helix, 43% strand	P31749

Ligands and binding sites

GVF · Benzene-1,2,3,4-tetrayl tetrakis[dihydrogen (phosphate)] · ligand · chains A
NA · Sodium ion · metal · chains A

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

Compared structures

2UVM · Structure of pkbalpha pH domain in complex with a novel inositol headgroup surrogate… · the same entry in another collection · chain A against A, TM-score 1.00
P31749 · AlphaFold monomer V2.0 prediction for rac-alpha SERINE/THREONINE- protein kinase (P31749) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 P31749
Elsewhere: RCSB PDB 2UVM · PDBe 2UVM · UniProt P31749

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