MolNFT v1 · #129389 · protein

Structure of the hmpv P oligomerization domain at 2.2 a

5OIY · Phosphoprotein: “Structure of the hmpv P oligomerization domain at 2.2 a”. X-ray diffraction, 2 pockets (best druggability 0.54). MolNFT v1 #129389 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5OIY
Type: protein
Length: 203 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoprotein
UniProt: Q91KZ5
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 6 distinct chains · 84% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Phosphoprotein	protein	26	77% helix, 0% strand	Q91KZ5
C	Phosphoprotein	protein	26	85% helix, 0% strand	Q91KZ5
D	Phosphoprotein	protein	24	88% helix, 0% strand	Q91KZ5
E, G	Phosphoprotein	protein	26	85% helix, 0% strand	Q91KZ5
F	Phosphoprotein	protein	24	83% helix, 0% strand	Q91KZ5
H	Phosphoprotein	protein	25	88% helix, 0% strand	Q91KZ5

Pockets

2 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	295	0.54	0.75	35	empty
2	73	0.36	0.77	19	empty

Interfaces

15 interfaces between chains.

A–B · 645 Å² buried · 2 hydrogen bonds · protein-protein
B–C · 637 Å² buried · 4 hydrogen bonds · protein-protein
G–H · 614 Å² buried · 3 hydrogen bonds · protein-protein
E–F · 594 Å² buried · 2 hydrogen bonds · protein-protein
E–H · 574 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

5OIY · Structure of the HMPV P oligomerization domain at 2.2 A · 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 Q91KZ5
Elsewhere: RCSB PDB 5OIY · PDBe 5OIY · UniProt Q91KZ5

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