MolNFT v1 · #116700 · protein

Aminopeptidase N (pepn) from francisella tularensis subsp. tularensis schu S4

5DLL: “Aminopeptidase N (pepn) from francisella tularensis subsp. tularensis schu S4”. X-ray diffraction, 4 ligands (ZN, NA, CL), 11 pockets (best druggability 0.80). MolNFT v1 #116700 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 5DLL
Type: protein
Length: 854 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminopeptidase N
EC: 3.4.11.2
UniProt: Q5NE65
Ligands: ZN, NA, CL, PO4
Pockets: 11 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminopeptidase N (EC 3.4.11.2)	protein	854	44% helix, 22% strand	Q5NE65

Ligands and binding sites

ZN · Zinc ion · metal · chains A
NA · Sodium ion · metal · chains A
CL · Chloride ion · ion · 15 copies · chains A
PO4 · Phosphate ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	943	0.80	0.82	91	empty
2	340	0.56	0.75	31	empty
3	236	0.54	0.77	35	empty
4	187	0.54	0.78	21	empty
5	79	0.44	0.81	21	CL

Compared structures

5DLL · Aminopeptidase N (pepN) from Francisella tularensis subsp. tularensis SCHU S4 · 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 Q5NE65
Elsewhere: RCSB PDB 5DLL · PDBe 5DLL · UniProt Q5NE65

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.