3NCL: MT-SP1

Crystal Structure of MT-SP1 bound to Benzamidine Phosphonate Inhibitor. Determined by X-ray diffraction at 1.19 Å resolution. Released 16 Feb 2011.

Method: X-ray diffraction
Resolution: 1.19 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,314
Mol. weight: 26.88 kDa
Ligands: CCZ
Released: 16 Feb 2011

Explore 3NCL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3NCL contains 9 α-helices and 22 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 9 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	12	1	1
β-strand	15-16	2	2
α-helix	17-18	2
β-strand	25-30	6	3
β-strand	34-41	8	3
β-strand	46-49	4	3
α-helix	51-54	4
β-strand	57	1	4
β-strand	60	1	4
α-helix	65-67	3
β-strand	68-72	5	3
β-strand	76	1	5
β-strand	86-95	10	3
β-strand	109-113	5	3
β-strand	127	1	2
α-helix	128-130	3
β-strand	140-145	6	2
β-strand	148	1	6
β-strand	162	1	6
β-strand	165	1	5
β-strand	167-173	7	2
α-helix	174-175	2
α-helix	176-182	7
β-strand	191-195	5	2
β-strand	202	1	1
α-helix	210	1
β-strand	211-215	5	2
β-strand	221-229	9	2
β-strand	240-244	5	2
α-helix	246-248	3
α-helix	249-256	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Suppressor of tumorigenicity 14 protein	A	protein	241	Homo sapiens	Q9Y5Y6 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3NCL_1 Suppressor of tumorigenicity 14 protein (chains A)
VVGGTDADEGEWPWQVSLHALGQGHICGASLISPNWLVSAAHCYIDDRGFRYSDPTQWTA
FLGLHDQSQRSAPGVQERRLKRIISHPFFNDFTFDYDIALLELEKPAEYSSMVRPISLPD
ASHVFPAGKAIWVTGWGHTQYGGTGALILQKGEIRVINQTTCENLLPQQITPRMMCVGFL
SGGVDSCQGDSGGPLSSVEADGRIFQAGVVSWGDGCAQRNKPGVYTRLPLFRDWIKENTG
V

Ligands and cofactors

ID	Name	Formula	Copies
CCZ	phenyl (4-carbamimidoylbenzyl)phosphonate	C14 H15 N2 O3 P	1

Water and common crystallization additives (FMT) are not listed.

Primary citation

Peptide length and leaving-group sterics influence potency of Peptide phosphonate protease inhibitors. Brown, C.M., Ray, M., Eroy-Reveles, A.A. et al. Chem Biol (2011) 18:48-57. DOI 10.1016/j.chembiol.2010.11.007 · PubMed

Other PDB entries of the same protein (UniProt Q9Y5Y6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3P8G 1.2 Å, Crystal Structure of MT-SP1 in complex with benzamidine
8G1W 1.2 Å, Crystal Structure Matriptase (C731S) in Complex with Inhibitor VD4162B
1EAX 1.3 Å, Crystal structure of MTSP1 (matriptase)
8G1V 1.35 Å, Crystal Structure Matriptase (C731S) in Complex with Inhibitor MM1132-2
4IS5 1.48 Å, Crystal Structure of the ligand-free inactive Matriptase
3NPS 1.5 Å, Crystal structure of membrane-type serine protease 1 (MT-SP1) in complex with the Fab…
6T9T 1.69 Å, Matriptase in complex with the synthetic inhibitor (S)-3-(3-(4-(3-(tert-butyl)ureido)pipe…
4JZ1 1.9 Å, Crystal Structure of Matriptase in complex with Inhibitor
4O9V 1.9 Å, Crystal structure of matriptase in complex with inhibitor
4R0I 1.9 Å, Crystal structure of matriptase in complex with inhibitor
6N4T 1.95 Å, Crystal structure of Matriptase1 in complex with a peptidomimetic benzothiazole
3P8F 2.0 Å, Crystal Structure of MT-SP1 in complex with SFTI-1

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