Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1TPK

CRYSTAL STRUCTURE OF THE KRINGLE-2 DOMAIN OF TISSUE PLASMINOGEN ACTIVATOR AT 2.4-ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0014909biological_processsmooth muscle cell migration
A0031639biological_processplasminogen activation
B0004252molecular_functionserine-type endopeptidase activity
B0014909biological_processsmooth muscle cell migration
B0031639biological_processplasminogen activation
C0004252molecular_functionserine-type endopeptidase activity
C0014909biological_processsmooth muscle cell migration
C0031639biological_processplasminogen activation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 83
ChainResidue
ALYS33
AVAL34
ATYR35
CASN26
CHOH90

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 83
ChainResidue
BHIS64
AASN26
BLYS33
BVAL34
BTYR35

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL C 83
ChainResidue
BASN26
BHOH88
CVAL34
CTYR35
CHIS64

Functional Information from PROSITE/UniProt
site_idPS00021
Number of Residues13
DetailsKRINGLE_1 Kringle domain signature. YCRNpdgdakp.WC
ChainResidueDetails
ATYR50-CYS63

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsSITE: Not glycosylated
ChainResidueDetails
AASN39
BASN39
CASN39

site_idSWS_FT_FI2
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:2513186
ChainResidueDetails
AASN5
BASN5
CASN5

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 798
ChainResidueDetails

site_idMCSA2
Number of Residues
DetailsM-CSA 798
ChainResidueDetails

site_idMCSA3
Number of Residues
DetailsM-CSA 798
ChainResidueDetails

224201

PDB entries from 2024-08-28

PDB statisticsPDBj update infoContact PDBjnumon