Research workbench

Crystal structure of porcine aminopeptidase N ectodomain in functional form

Analyse Crystal structure of porcine aminopeptidase N ectodomain in functional form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5Z65
Type: protein
Length: 900 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminopeptidase
EC: 3.4.11.-
UniProt: K7GMF9
Ligands: NAG, ZN
Pockets: 8 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminopeptidase (EC 3.4.11.-)	protein	900	44% helix, 20% strand	K7GMF9

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 19 copies · chains A
ZN · Zinc ion · metal · chains A

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

Pockets

8 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	672	0.66	0.75	52	empty
2	453	0.62	0.76	38	empty
3	390	0.60	0.77	48	empty
4	314	0.52	0.74	36	empty
5	103	0.40	0.77	18	empty

Modifications

Observed in the structure: 9 glycan, 2 disulfide (N-glycosylation, disulfide).

Compared structures

5Z65 · Crystal structure of porcine aminopeptidase N ectodomain in functional form · 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 K7GMF9
Elsewhere: RCSB PDB 5Z65 · PDBe 5Z65 · UniProt K7GMF9

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