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5LYO

Crystal structure of the zymogen matriptase catalytic domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue SO4 A 901
ChainResidue
AHIS656
AALA805
ATRP826
AGLY827

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 902
ChainResidue
AARG684
AHIS633
ALEU635
AGLY636
AGLN637
AGLY638

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 903
ChainResidue
AASP734
AHIS737
APHE819

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 904
ChainResidue
AARG611
AGLN612
AARG833
BGLN832
BASN834
BLYS835

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 905
ChainResidue
AHIS752
ATHR758
CGLN772

site_idAC6
Number of Residues2
Detailsbinding site for residue SO4 A 906
ChainResidue
AGLU691
AARG692

site_idAC7
Number of Residues2
Detailsbinding site for residue SO4 A 907
ChainResidue
AVAL770
AHOH1002

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 B 901
ChainResidue
BHIS656
BALA805
BTRP826
BGLY827

site_idAC9
Number of Residues5
Detailsbinding site for residue SO4 B 902
ChainResidue
BHIS633
BGLY636
BGLN637
BGLY638
BARG684

site_idAD1
Number of Residues3
Detailsbinding site for residue SO4 B 903
ChainResidue
BGLN690
BGLU691
BARG692

site_idAD2
Number of Residues4
Detailsbinding site for residue SO4 B 904
ChainResidue
BARG833
BASN834
BHOH1004
BHOH1024

site_idAD3
Number of Residues4
Detailsbinding site for residue SO4 B 905
ChainResidue
AGLN772
BHIS752
BTHR758
BHOH1013

site_idAD4
Number of Residues4
Detailsbinding site for residue SO4 C 901
ChainResidue
CHIS656
CALA805
CTRP826
CGLY827

site_idAD5
Number of Residues5
Detailsbinding site for residue SO4 C 902
ChainResidue
APHE706
CPRO648
CALA721
CGLU722
CTYR723

site_idAD6
Number of Residues3
Detailsbinding site for residue SO4 C 903
ChainResidue
CPRO733
CASP734
CHIS737

site_idAD7
Number of Residues4
Detailsbinding site for residue SO4 C 904
ChainResidue
BGLN772
CHIS752
CTHR758
CHOH1008

site_idAD8
Number of Residues8
Detailsbinding site for residue SO4 C 905
ChainResidue
AARG833
AHOH1006
AHOH1024
AHOH1029
AHOH1047
AHOH1054
BARG833
CARG833

site_idAD9
Number of Residues3
Detailsbinding site for residue SO4 C 906
ChainResidue
CTHR610
CARG833
CASN834

site_idAE1
Number of Residues4
Detailsbinding site for residue SO4 C 907
ChainResidue
CARG607
CPHE609
CGLU625
CTRP626

site_idAE2
Number of Residues5
Detailsbinding site for residue SO4 C 908
ChainResidue
CVAL689
CGLN690
CGLU691
CARG692
CGLU722

site_idAE3
Number of Residues1
Detailsbinding site for residue SO4 C 909
ChainResidue
CSER725

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
AVAL652-CYS657

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS656
AASP711
AALA805
BHIS656
BASP711
BALA805
CHIS656
CASP711
CALA805

site_idSWS_FT_FI2
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AGLN772
BGLN772
CGLN772

220113

PDB entries from 2024-05-22

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