MolNFT v1 · #70885 · protein

Crystal structure of tripeptidyl peptidase 2 (tpp II)

3LXU · Tripeptidyl-peptidase 2: “Crystal structure of tripeptidyl peptidase 2 (tpp II)”. X-ray diffraction, 20 pockets (best druggability 0.80). MolNFT v1 #70885 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3LXU
Type: protein
Length: 1,217 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tripeptidyl-peptidase 2
EC: 3.4.14.10
UniProt: Q9V6K1
Pockets: 20 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Tripeptidyl-peptidase 2 (EC 3.4.14.10)	protein	1217	26% helix, 27% strand	Q9V6K1

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	466	0.80	0.88	59	empty
2	1086	0.79	0.80	106	empty
3	152	0.75	0.93	33	empty
4	392	0.63	0.78	42	empty
5	305	0.61	0.78	38	empty

Modifications

Observed in the structure: 25 modified (engineered).

Compared structures

3LXU · Crystal Structure of Tripeptidyl Peptidase 2 (TPP II) · the same entry in another collection · chain X against X, TM-score 1.00
Q9V6K1 · AlphaFold monomer V2.0 prediction for tripeptidyl-peptidase 2 (Q9V6K1) · a predicted model of the same protein · chain X against A, TM-score 0.98

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 Q9V6K1
Elsewhere: RCSB PDB 3LXU · PDBe 3LXU · UniProt Q9V6K1

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