Structure for peptidase S01.233: plasmin

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Pharma

PDB	Organism	Resolution	Comment
1BUI_A	Homo sapiens	2.65 Å	catalytic domain; complex with staphylokinase and Glu-Gly-deoxo-methylArg
One molecule of the dimer is shown. Staphylokinase is not shown. Catalytic residues are shown in ball-and-stick representation: His622 in purple, Asp665 in pink and Ser760 in orange. Glu-Gly-deoxomethylarginine is shown in grey in ball-and-stick representation.

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TERTIARY STRUCTURE DATA
Comment	Resolution	PDB	PDBe	SCOP	CATH	PDBSum	Proteopedia	Reference
Homo sapiens
NMR structure of kringle 2 domain	0.00 Å	1B2I	1B2I	1B2I	1B2I	1B2I	1B2I	Marti et al., 1999
catalytic domain; complex with streptokinase	2.90 Å	1BML	1BML	1BML	1BML	1BML	1BML	Wang et al., 1998
catalytic domain; complex with staphylokinase and Glu-Gly-deoxo-methylArg	2.65 Å	1BUI	1BUI	1BUI	1BUI	1BUI	1BUI	Parry et al., 1998
kringle 1 domain; complex with epsilon-aminocaproic acid	2.10 Å	1CEA	1CEA	1CEA	1CEA	1CEA	1CEA	Mathews et al., 1996
kringle 1 domain; complex with trans-4-aminomethylcyclohexane-1-carboxylic acid	2.10 Å	1CEB	1CEB	1CEB	1CEB	1CEB	1CEB	Mathews et al., 1996
catalytic domain	2.00 Å	1DDJ	1DDJ	1DDJ	1DDJ	1DDJ	1DDJ	Wang et al., 2000
NMR structure; kringle 1	0.00 Å	1HPJ	1HPJ	1HPJ	1HPJ	1HPJ	1HPJ	Rejante & Llinas, 1994
NMR structure; kringle 1	0.00 Å	1HPK	1HPK	1HPK	1HPK	1HPK	1HPK	Rejante & Llinas, 1994
mature peptidase	2.70 Å	1I5K	1I5K	1I5K	1I5K	1I5K	1I5K	Rios-Steiner et al., 2001
mature peptidase	1.75 Å	1KI0	1KI0	1KI0	1KI0	1KI0	1KI0	Abad et al., 2002
kringle 4	1.67 Å	1KRN	1KRN	1KRN	1KRN	1KRN	1KRN	Stec et al., 1997
microplasminogen; complex with streptokinase alpha domain	2.30 Å	1L4D	1L4D	1L4D	1L4D	1L4D	1L4D	Wakeham et al., 2002
microplasminogen; complex with streptokinase alpha domain in the presence cadmium ions	2.80 Å	1L4Z	1L4Z	1L4Z	1L4Z	1L4Z	1L4Z	Wakeham et al., 2002
kringle 4	1.90 Å	1PK4	1PK4	1PK4	1PK4	1PK4	1PK4	Mulichak et al., 1991
kringle 1	2.48 Å	1PKR	1PKR	1PKR	1PKR	1PKR	1PKR	Wu et al., 1994
kringle 4	2.25 Å	1PMK	1PMK	1PMK	1PMK	1PMK	1PMK	Padmanabhan et al., 1994
proenzyme form of catalytic domain, complex with streptokinase	2.00 Å	1QRZ	1QRZ	1QRZ	1QRZ	1QRZ	1QRZ	Peisach et al., 1999
human plasminogen catalytic domain, k698m mutant	2.30 Å	1RJX	1RJX	1RJX	1RJX	1RJX	1RJX	Terzyan et al., 2004
mature peptidase	2.30 Å	2DOH	2DOH	2DOH	2DOH	2DOH	2DOH	Cnudde et al., 2006
mature peptidase	3.10 Å	2DOI	2DOI	2DOI	2DOI	2DOI	2DOI	Cnudde et al., 2006
mature peptidase	0.00 Å	2KNF	2KNF	2KNF	2KNF	2KNF	2KNF	Battistel et al., 2009
mature peptidase	0.00 Å	2L0S	2L0S	2L0S	2L0S	2L0S	2L0S	Christen et al., 2010
kringle 4 complex with epsilon-aminocaproic acid	2.25 Å	2PK4	2PK4	2PK4	2PK4	2PK4	2PK4	Wu et al., 1991
mature peptidase	2.78 Å	3UIR	3UIR	3UIR	3UIR	3UIR	3UIR	Millers et al., 2013
mature peptidase	3.49 Å	4A5T	4A5T	4A5T	4A5T	4A5T	4A5T	Xue et al., 2012
mature peptidase	1.78 Å	4CIK	4CIK	4CIK	4CIK	4CIK	4CIK	Cheng et al., 2014
mature peptidase	2.03 Å	4DCB	4DCB	4DCB	4DCB	4DCB	4DCB	Eren & van, 2012
mature peptidase	2.45 Å	4DUR	4DUR	4DUR	4DUR	4DUR	4DUR	Law et al., 2012
mature peptidase	5.20 Å	4DUU	4DUU	4DUU	4DUU	4DUU	4DUU	Law et al., 2012
kringle 5 domain only	1.66 Å	5HPG	5HPG	5HPG	5HPG	5HPG	5HPG	Chang et al., 1998
protease inhibitor	1.38 Å	5UGD	5UGD	5UGD	5UGD	5UGD	5UGD
protease inhibitor	1.20 Å	5UGG	5UGG	5UGG	5UGG	5UGG	5UGG
highly potent and selective plasmin inhibitors based on the sunflower trypsin inhibitor-1 scaffold attenuate fibrinolysis in plasma ***caveat 6d3x entry contains improper peptide linkages.	1.80 Å	6D3X	6D3X	6D3X	6D3X	6D3X	6D3X
highly potent and selective plasmin inhibitors based on the sunflower trypsin inhibitor-1 scaffold attenuate fibrinolysis in plasma ***caveat 6d3y entry contains improper peptide linkages.	1.32 Å	6D3Y	6D3Y	6D3Y	6D3Y	6D3Y	6D3Y
protease sfti complex	2.00 Å	6D3Z	6D3Z	6D3Z	6D3Z	6D3Z	6D3Z
highly potent and selective plasmin inhibitors based on the sunflower trypsin inhibitor-1 scaffold attenuate fibrinolysis in plasma ***caveat 6d40 entry contains improper peptide linkages.	1.43 Å	6D40	6D40	6D40	6D40	6D40	6D40