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Partial structure of the C-terminal domain of the HPIV4B phosphoprotein, fused to mbp.

Analyse Partial structure of the C-terminal domain of the HPIV4B phosphoprotein, fused… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KYE
Type: protein
Length: 400 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Maltose-binding periplasmic protein, phosphoprotein, chimeric construct
UniProt: P0AEX9, P21738
Ligands: GLC
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Maltose-binding periplasmic protein, phosphoprotein, chimeric construct	protein	400	48% helix, 19% strand	P0AEX9, P21738

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	257	0.69	0.85	24	GLC
2	232	0.50	0.75	32	empty
3	68	0.36	0.77	17	empty
4	64	0.27	0.72	15	empty

Compared structures

4KYE · Partial Structure of the C-terminal domain of the HPIV4B phosphoprotein, fused to MBP. · 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 P0AEX9
Every structure of UniProt P21738
Elsewhere: RCSB PDB 4KYE · PDBe 4KYE · UniProt P0AEX9 · UniProt P21738

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