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Crystal structure of human dipeptidase 3

Analyse Crystal structure of human dipeptidase 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6VGO
Type: protein
Length: 350 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dipeptidase 3
EC: 3.4.13.19
UniProt: Q9H4B8
Pockets: 2 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dipeptidase 3 (EC 3.4.13.19)	protein	350	46% helix, 16% strand	Q9H4B8

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	81	0.34	0.75	21	empty
2	66	0.29	0.74	21	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6VGO · Crystal Structure of Human Dipeptidase 3 · the same entry in another collection · chain A against A, TM-score 1.00
Q9H4B8 · AlphaFold monomer V2.0 prediction for dipeptidase 3 (Q9H4B8) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9H4B8
Elsewhere: RCSB PDB 6VGO · PDBe 6VGO · UniProt Q9H4B8

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