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1PML

KRINGLE-KRINGLE INTERACTIONS IN MULTIMER KRINGLE STRUCTURES

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 Residues4
DetailsBINDING SITE FOR RESIDUE CL A 289
ChainResidue
AVAL34
ATYR35
AHIS64
CASN26

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 290
ChainResidue
AASN26
BLYS33
BVAL34
BTYR35
BHIS64

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C 291
ChainResidue
BASN26
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
AASN41
BASN41
CASN41

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

230744

PDB entries from 2025-01-29

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