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Crystal structure of MTSP1 (matriptase)

Analyse Crystal structure of MTSP1 (matriptase) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EAX
Type: protein
Length: 241 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Suppressor of tumorigenicity 14
EC: 3.4.21.-
UniProt: Q9Y5Y6
Ligands: BEN, SO4
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Suppressor of tumorigenicity 14 (EC 3.4.21.-)	protein	241	10% helix, 37% strand	Q9Y5Y6

Ligands and binding sites

BEN · Benzamidine · ligand · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	112	0.39	0.75	30	SO4, BEN

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1EAX · Crystal structure of MTSP1 (matriptase) · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y5Y6 · AlphaFold monomer V2.0 prediction for suppressor of tumorigenicity 14 protein (Q9Y5Y6) · 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 Q9Y5Y6
Elsewhere: RCSB PDB 1EAX · PDBe 1EAX · UniProt Q9Y5Y6

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