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Crystal structure of the core catalytic domain of human inositol phosphate multikinase in complex with kaempferol

Analyse Crystal structure of the core catalytic domain of human inositol phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6M8B
Type: protein
Length: 238 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inositol polyphosphate MULTIKINASE,INOSITOL polyphosphate multikinase
EC: 2.7.1.151
UniProt: Q8NFU5
Ligands: KMP
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Inositol polyphosphate MULTIKINASE,INOSITOL polyphosphate multikinase (EC 2.7.1.151)	protein	238	35% helix, 26% strand	Q8NFU5

Ligands and binding sites

KMP · 3,5,7-trihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one · ligand · 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	345	0.64	0.79	49	KMP

Compared structures

6M8B · Crystal structure of the core catalytic domain of human inositol phosphate multikinase in… · the same entry in another collection · chain A against A, TM-score 1.00
Q8NFU5 · AlphaFold monomer V2.0 prediction for inositol polyphosphate multikinase (Q8NFU5) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q8NFU5
Elsewhere: RCSB PDB 6M8B · PDBe 6M8B · UniProt Q8NFU5

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