1oc0

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File:1oc0.png

1oc0, resolution 2.28Å ()

Related:

1a7c, 1b3k, 1c5g, 1db2, 1dvm, 1dvn, 1lj5, 9pai

Structural annotation:
Resources:	CATH : 1Oc0A02, 1Oc0A01 InterPro : Ipr000215, Ipr001212, Ipr000585 Pfam : PF00079, PF01033 SCOP : d1oc0a_, d1oc0b_ UniProt : P05121, P04004

Functional annotation:
Cellular component:	extracellular region extracellular space proteinaceous extracellular matrix
Biological process:	blood coagulation regulation of angiogenesis fibrinolysis cell adhesion immune response cell-matrix adhesion
Molecular function:	protein binding endopeptidase inhibitor activity protease binding plasminogen activator activity serine-type endopeptidase inhibitor activity metal ion binding heparin binding catalytic activity

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

PLASMINOGEN ACTIVATOR INHIBITOR-1 COMPLEX WITH SOMATOMEDIN B DOMAIN OF VITRONECTINPLASMINOGEN ACTIVATOR INHIBITOR-1 COMPLEX WITH SOMATOMEDIN B DOMAIN OF VITRONECTIN

Template:ABSTRACT PUBMED 12808446

About this StructureAbout this Structure

1OC0 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration., Zhou A, Huntington JA, Pannu NS, Carrell RW, Read RJ, Nat Struct Biol. 2003 Jul;10(7):541-4. PMID:12808446

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OCA