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3E1Z

Crystal structure of the parasite protesase inhibitor chagasin in complex with papain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004869molecular_functioncysteine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0009986cellular_componentcell surface
A0020016cellular_componentciliary pocket
A0031410cellular_componentcytoplasmic vesicle
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 111
ChainResidue
AGLU23
AHIS72
AHIS74
AFMT113

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT A 112
ChainResidue
BGLY101

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 113
ChainResidue
AZN111
AHOH141
BTYR61
AGLU23
APHE58
AHIS72
AHIS74

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 114
ChainResidue
APHE34
ASER97
AHIS98
AASP99
AHOH148
BASN18

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ACY B 213
ChainResidue
AASN29
ATHR31
ATHR32
AGLY66
BGLN19
BGLY23
BSER24
BCYS25
BASP158
BHIS159

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 214
ChainResidue
BSER124
BASN127
BGLN128
BTYR208
BHOH380

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT B 215
ChainResidue
BTYR78
BHIS81
BHOH382

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT B 216
ChainResidue
BARG98
BHOH382

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT B 217
ChainResidue
BHOH400

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT B 218
ChainResidue
AGLU20
BGLN92
BHOH390

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT B 219
ChainResidue
BLYS190

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 220
ChainResidue
BGLN9
BILE40
BHOH298
BHOH400
BHOH441

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGsCGSCWAfSA
ChainResidueDetails
BGLN19-ALA30

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VDHAVAAVGYG
ChainResidueDetails
BVAL157-GLY167

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YILiKNSWgtgWGenGYIrI
ChainResidueDetails
BTYR170-ILE189

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000269|PubMed:5681232, ECO:0000269|PubMed:6502713, ECO:0000269|PubMed:952885, ECO:0000305|PubMed:1860874, ECO:0007744|PDB:1PAD, ECO:0007744|PDB:9PAP
ChainResidueDetails
BCYS25

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089, ECO:0000269|PubMed:6502713, ECO:0000269|PubMed:952885, ECO:0007744|PDB:1PAD, ECO:0007744|PDB:9PAP
ChainResidueDetails
BHIS159

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090, ECO:0000269|PubMed:5681232, ECO:0000269|PubMed:6502713, ECO:0000269|PubMed:952885, ECO:0007744|PDB:1PAD, ECO:0007744|PDB:9PAP
ChainResidueDetails
BASN175

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: covalent => ECO:0000269|PubMed:8416808, ECO:0007744|PDB:1POP
ChainResidueDetails
BCYS25

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BASN175
BCYS25
BHIS159

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BGLN19
BCYS25
BHIS159

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BASN175
BGLN19
BHIS159

site_idMCSA1
Number of Residues4
DetailsM-CSA 174
ChainResidueDetails
BGLN19electrostatic stabiliser, hydrogen bond donor
BCYS25electrostatic stabiliser
BHIS159electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BASN175activator, electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2024-07-24

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