MolNFT v1 · #71977 · protein

APPEP_PEPCLOSE closed state

3MUN · Prolyl endopeptidase: “APPEP_PEPCLOSE closed state”. X-ray diffraction, 3 ligands (GLC, FRU, SO4), 7 pockets (best druggability 0.73). MolNFT v1 #71977 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3MUN
Type: protein
Length: 684 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prolyl endopeptidase
UniProt: Q9X6R4
Ligands: GLC, FRU, SO4
Pockets: 7 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Prolyl endopeptidase	protein	684	22% helix, 34% strand	Q9X6R4

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · chains A
FRU · beta-D-fructofuranose · sugar · chains A
SO4 · Sulfate ion · ion · 6 copies · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	897	0.73	0.77	114	GOL
2	396	0.68	0.80	38	empty
3	76	0.47	0.82	19	empty
4	56	0.35	0.79	18	empty
5	58	0.33	0.77	15	empty

Compared structures

3MUN · APPEP_PEPCLOSE closed state · 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 Q9X6R4
Elsewhere: RCSB PDB 3MUN · PDBe 3MUN · UniProt Q9X6R4

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