3P8F

Crystal Structure of MT-SP1 in complex with SFTI-1

PDB DOI: https://doi.org/10.2210/pdb3P8F/pdb

Classification: HYDROLASE/HYDROLASE INHIBITOR
Organism(s): Homo sapiens, Helianthus annuus
Expression System: Saccharomyces cerevisiae
Mutation(s): Yes

Deposited: 2010-10-13 Released: 2011-08-10
Deposition Author(s): Yuan, C., Huang, M., Chen, L.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.00 Å
R-Value Free: 0.245
R-Value Work: 0.192
R-Value Observed: 0.194

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.2 of the entry. See complete history.

Literature

Structure of catalytic domain of Matriptase in complex with Sunflower trypsin inhibitor-1.

Yuan, C., Chen, L., Meehan, E.J., Daly, N., Craik, D.J., Huang, M., Ngo, J.C.

(2011) BMC Struct Biol 11: 30-30

PubMed: 21693064 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1186/1472-6807-11-30
Primary Citation of Related Structures:
3P8F, 3P8G

PubMed Abstract:
Matriptase is a type II transmembrane serine protease that is found on the surfaces of epithelial cells and certain cancer cells. Matriptase has been implicated in the degradation of certain extracellular matrix components as well as the activation of various cellular proteins and proteases, including hepatocyte growth factor and urokinase. Sunflower trypsin inhibitor-1 (SFTI-1), a cyclic peptide inhibitor originally isolated from sunflower seeds, exhibits potent inhibitory activity toward matriptase.

Organizational Affiliation

State Key Lab of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou, Fujian 350002, China.

Macromolecule Content

Total Structure Weight: 28.32 kDa
Atom Count: 2,090
Modelled Residue Count: 255
Deposited Residue Count: 255
Unique protein chains: 2

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
ST14 protein	A	241	Homo sapiens	Mutation(s): 1 Gene Names: ST14 EC: 3.4.21.109
UniProt & NIH Common Fund Data Resources
Find proteins for Q9Y5Y6 (Homo sapiens) Explore Q9Y5Y6 Go to UniProtKB: Q9Y5Y6
PHAROS: Q9Y5Y6 GTEx: ENSG00000149418
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q9Y5Y6
Sequence Annotations Expand
Reference Sequence

Find similar proteins by: Sequence | 3D Structure

Entity ID: 2
Molecule	Chains	Sequence Length	Organism	Details	Image
Trypsin inhibitor 1	B [auth I]	14	Helianthus annuus	Mutation(s): 0
UniProt
Find proteins for Q4GWU5 (Helianthus annuus) Explore Q4GWU5 Go to UniProtKB: Q4GWU5
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q4GWU5
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
GSH Query on GSH Download Ideal Coordinates CCD File SDF format, chain C [auth A] MOL2 format, chain C [auth A]	C [auth A]	GLUTATHIONE C₁₀ H₁₇ N₃ O₆ S RWSXRVCMGQZWBV-WDSKDSINSA-N		Interactions Focus chain C [auth A] Interactions & Density Focus chain C [auth A]

Biologically Interesting Molecules (External Reference) 1 Unique

Entity ID: 2
ID	Chains	Name	Type/Class	2D Diagram	3D Interactions
PRD_001097 Query on PRD_001097	B [auth I]	Trypsin inhibitor 1	Polypeptide / Trypsin inhibitor		Interactions Focus chain B [auth I] Interactions & Density Focus chain B [auth I]