1OWE: Urokinase-type plasminogen activator

Substituted 2-Naphthamidine inhibitors of urokinase. Determined by X-ray diffraction at 1.6 Å resolution. Released 30 Sept 2003.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,194
Mol. weight: 28.21 kDa
Ligands: 675
Released: 30 Sept 2003

Explore 1OWE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1OWE contains 11 α-helices and 20 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: 11 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	1
β-strand	5-6	2	2
α-helix	9-11	3
β-strand	15-21	7	3
α-helix	22	1
β-strand	29-43	11	3
β-strand	48-51	4	3
α-helix	53-55	3
α-helix	62-65	3
β-strand	67-71	5	3
β-strand	76	1	4
β-strand	86-95	10	3
β-strand	100-101	2	5
β-strand	106-107	2	5
β-strand	111-116	6	3
β-strand	133	1	2
α-helix	134-136	3
α-helix	140-142	3
β-strand	146-151	6	2
α-helix	162-163	2
β-strand	165	1	4
β-strand	168-175	8	2
α-helix	177-180	4
α-helix	187-189	3
β-strand	194-198	5	2
β-strand	205	1	1
β-strand	214-219	6	2
β-strand	222-231	10	2
β-strand	242-246	5	2
α-helix	247-250	4
α-helix	251-257	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Urokinase-type plasminogen activator	A	protein	245	Homo sapiens	P00749 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1OWE_1 Urokinase-type plasminogen activator (chains A)
IIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLMSPCWVISATHCFIDYPKKEDYIVY
LGRSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTI
CLPSMYNDPQFGTSCEITGFGKEQSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTK
MLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPW
IRSHT

Ligands and cofactors

ID	Name	Formula	Copies
675	6-[(Z)-amino(imino)methyl]-N-phenyl-2-naphthamide	C18 H15 N3 O	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Identification of Novel Binding Interactions in the Development of Potent, Selective 2-Naphthamidine Inhibitors of Urokinase. Synthesis, Structural Analysis, and SAR of N-Phenyl Amide 6-Substitution. Wendt, M.D., Rockway, T.W., Geyer, A. et al. J Med Chem (2004) 47:303-324. DOI 10.1021/jm0300072 · PubMed

Other PDB entries of the same protein (UniProt P00749 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5YC6 1.18 Å, The crystal structure of uPA in complex with 4-Bromobenzylamirne at pH4.6
4ZKO 1.29 Å, The crystal structure of upain-1-W3A in complex with uPA at pH7.4
4ZKN 1.36 Å, The crystal structure of upain-1-W3A in complex with uPA at pH5.5
4ZKR 1.36 Å, The crystal structure of upain-1-W3A in complex with uPA at pH9.0
6XVD 1.4 Å, Crystal structure of complex of urokinase and a upain-1 variant(W3F) in pH7.4 condition
2O8T 1.45 Å, Crystal Structure and Binding Epitopes of Urokinase-type Plasminogen Activator…
3MHW 1.45 Å, The complex crystal Structure of Urokianse and 2-Aminobenzothiazole
5Z1C 1.45 Å, The crystal structure of uPA in complex with 4-Iodobenzylamine at pH7.4
5WXF 1.46 Å, Crystal structure of uPA in complex with upain-2-2
4MNW 1.49 Å, Crystal structure of urokinase-type plasminogen activator (uPA) complexed with bicyclic…
1GJ7 1.5 Å, Engineering inhibitors highly selective for the S1 sites of SER190 trypsin-like serine…
4XSK 1.5 Å, Structure of PAItrap, an uPA mutant

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