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1RJX

Human PLASMINOGEN CATALYTIC DOMAIN, K698M MUTANT

Functional Information from GO Data
ChainGOidnamespacecontents
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 201
ChainResidue
BHOH108
BHOH115
BHOH154
BPRO595
BARG789
BASN790

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 202
ChainResidue
BGLN721
BSER722
BHOH103
BHIS629
BARG644

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 203
ChainResidue
BHOH134
BSER636
BARG637
BLYS651

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 204
ChainResidue
BARG644
BLYS661

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 205
ChainResidue
BHOH112
BSO4207
BHIS571
BGLU627
BLYS661
BARG719

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 206
ChainResidue
BHOH147
BARG712
BTYR713
BGLU714

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 207
ChainResidue
BHOH10
BHOH105
BSO4205
BPRO570
BARG719

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 208
ChainResidue
BHOH55
BHOH55
BARG677
BPRO703
BHIS729
BHIS729
BLEU730
BALA731

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
BLEU599-CYS604

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLV
ChainResidueDetails
BASP735-VAL746

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
BHIS603
BASP646
BSER741

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by plasminogen activator
ChainResidueDetails
BALA561

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9201958
ChainResidueDetails
BSER578

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER669

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BHIS603
BASP646

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BSER741
BGLY742

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BSER741
BGLY739

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BHIS603
BSER741
BASP646

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BHIS603
BSER741
BASP646
BGLY742

site_idCSA6
Number of Residues7
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BCYS737
BHIS603
BSER741
BASP740
BASP646
BGLY739
BGLN738

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BHIS603
BSER741
BGLY739
BASP646

site_idMCSA1
Number of Residues4
DetailsM-CSA 425
ChainResidueDetails
BHIS603proton shuttle (general acid/base)
BASP646electrostatic stabiliser, modifies pKa
BSER741covalent catalysis, proton shuttle (general acid/base)
BGLY742electrostatic stabiliser

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PDB entries from 2024-11-06

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