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Structure of ligand free human DPP3 in closed form.

Analyse Structure of ligand free human DPP3 in closed form. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EGY
Type: protein
Length: 724 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dipeptidyl peptidase 3
EC: 3.4.14.4
UniProt: Q9NY33
Ligands: ZN, MG
Pockets: 4 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dipeptidyl peptidase 3 (EC 3.4.14.4)	protein	724	48% helix, 16% strand	Q9NY33

Ligands and binding sites

ZN · Zinc ion · metal · chains A
MG · Magnesium ion · metal · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	846	0.88	0.91	119	ZN
2	126	0.68	0.90	31	empty
3	85	0.43	0.79	25	MG
4	52	0.24	0.73	13	empty

Compared structures

5EGY · Structure of ligand free human DPP3 in closed form. · the same entry in another collection · chain A against A, TM-score 1.00
Q9NY33 · AlphaFold monomer V2.0 prediction for dipeptidyl peptidase 3 (Q9NY33) · a predicted model of the same protein · 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 Q9NY33
Elsewhere: RCSB PDB 5EGY · PDBe 5EGY · UniProt Q9NY33

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