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1L4Z

X-RAY CRYSTAL STRUCTURE OF THE COMPLEX OF MICROPLASMINOGEN WITH ALPHA DOMAIN OF STREPTOKINASE IN THE PRESENCE CADMIUM IONS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0005576cellular_componentextracellular region
B0031639biological_processplasminogen activation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD B 201
ChainResidue
BASP32
BHIS140
BHOH203
BHOH204
BHOH205

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CD B 202
ChainResidue
BSER21

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 103
ChainResidue
AHOH68
AHIS569

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 104
ChainResidue
AHOH60
AHIS571
AGLU627
AHOH50

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 105
ChainResidue
AHOH2
AHOH6
ACD106
AHIS603
AGLU606
AASP646

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 106
ChainResidue
ACD105
AHIS603
AGLU606
AGLU724

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU599-CYS604

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues227
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Cleavage; by plasminogen activator"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"9201958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qrz
ChainResidueDetails
AHIS603
AASP646

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qrz
ChainResidueDetails
AALA741
AGLY742

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qrz
ChainResidueDetails
AALA741
AGLY739

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qrz
ChainResidueDetails
AHIS603
AALA741
AASP646
AGLY742

site_idCSA5
Number of Residues7
DetailsAnnotated By Reference To The Literature 1qrz
ChainResidueDetails
ACYS737
AHIS603
AALA741
AASP740
AASP646
AGLY739
AGLN738

site_idMCSA1
Number of Residues4
DetailsM-CSA 425
ChainResidueDetails
AHIS603proton shuttle (general acid/base)
AASP646electrostatic stabiliser, modifies pKa
AALA741covalent catalysis, proton shuttle (general acid/base)
AGLY742electrostatic stabiliser

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PDB entries from 2025-07-30

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