1C5N

STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR

External Resource: Annotation


Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
B [auth H]d1c5n.1 All beta proteins Trypsin-like serine proteases Trypsin-like serine proteases Eukaryotic proteases Thrombin (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
A [auth L]d1c5n.1 All beta proteins Trypsin-like serine proteases Trypsin-like serine proteases Eukaryotic proteases Thrombin (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
B [auth H]SCOP2B SuperfamilyTrypsin-like serine proteases 8042154 3000114 SCOP2B (2022-06-29)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B [auth H]2.40.10.10 Mainly Beta Beta Barrel Thrombin, subunit H Trypsin-like serine proteasesCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
B [auth H]PF00089Trypsin (Trypsin)Trypsin- Domain
A [auth L]PF09396Thrombin light chain (Thrombin_light)Thrombin light chainThrombin is an enzyme that cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII. Prothrombin is activated on the surface of a phospholipid membrane where factor Xa removes the activation peptide and cleave ...Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII. Prothrombin is activated on the surface of a phospholipid membrane where factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. This domain corresponds to the light chain of thrombin.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
B [auth H]Thrombin heavy chain
A [auth L]Thrombin light chain
C [auth I]Hirudin -

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
B [auth H]IPR018992Thrombin light chainDomain
B [auth H]IPR037111Thrombin light chain domain superfamilyHomologous Superfamily
B [auth H]IPR003966Prothrombin/thrombinFamily
B [auth H]IPR018114Serine proteases, trypsin family, histidine active siteActive Site
B [auth H]IPR009003Peptidase S1, PA clanHomologous Superfamily
B [auth H]IPR033116Serine proteases, trypsin family, serine active siteActive Site
B [auth H]IPR001254Serine proteases, trypsin domainDomain
B [auth H]IPR035972Gamma-carboxyglutamic acid-rich (GLA) domain superfamilyHomologous Superfamily
B [auth H]IPR000001KringleDomain
B [auth H]IPR000294Gamma-carboxyglutamic acid-rich (GLA) domainDomain
B [auth H]IPR051659Serine Protease S1 Domain-Containing ProteinFamily
B [auth H]IPR018056Kringle, conserved siteConserved Site
B [auth H]IPR013806Kringle-like foldHomologous Superfamily
B [auth H]IPR038178Kringle superfamilyHomologous Superfamily
B [auth H]IPR001314Peptidase S1A, chymotrypsin familyFamily
B [auth H]IPR043504Peptidase S1, PA clan, chymotrypsin-like foldHomologous Superfamily
A [auth L]IPR018992Thrombin light chainDomain
A [auth L]IPR037111Thrombin light chain domain superfamilyHomologous Superfamily
A [auth L]IPR003966Prothrombin/thrombinFamily
A [auth L]IPR018114Serine proteases, trypsin family, histidine active siteActive Site
A [auth L]IPR009003Peptidase S1, PA clanHomologous Superfamily
A [auth L]IPR033116Serine proteases, trypsin family, serine active siteActive Site
A [auth L]IPR001254Serine proteases, trypsin domainDomain
A [auth L]IPR035972Gamma-carboxyglutamic acid-rich (GLA) domain superfamilyHomologous Superfamily
A [auth L]IPR000001KringleDomain
A [auth L]IPR000294Gamma-carboxyglutamic acid-rich (GLA) domainDomain
A [auth L]IPR051659Serine Protease S1 Domain-Containing ProteinFamily
A [auth L]IPR018056Kringle, conserved siteConserved Site
A [auth L]IPR013806Kringle-like foldHomologous Superfamily
A [auth L]IPR038178Kringle superfamilyHomologous Superfamily
A [auth L]IPR001314Peptidase S1A, chymotrypsin familyFamily
A [auth L]IPR043504Peptidase S1, PA clan, chymotrypsin-like foldHomologous Superfamily
C [auth I]IPR011061Hirudin/antistatinHomologous Superfamily
C [auth I]IPR000429Proteinase inhibitor I14, hirudinFamily
C [auth I]IPR024793Thrombin inhibitor hirudinHomologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
B [auth H]Pharos:  P00734
A [auth L]Pharos:  P00734

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
C [auth I]TYS Parent Component: TYR

RESID:  AA0172

PSI-MOD :  O4'-sulfo-L-tyrosine MOD:00181