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4AXM

TRIAZINE CATHEPSIN INHIBITOR COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
F0006508biological_processproteolysis
F0008234molecular_functioncysteine-type peptidase activity
I0006508biological_processproteolysis
I0008234molecular_functioncysteine-type peptidase activity
L0006508biological_processproteolysis
L0008234molecular_functioncysteine-type peptidase activity
O0006508biological_processproteolysis
O0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 1221
ChainResidue
AASN18
AGLY20

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE V65 A 1222
ChainResidue
ALEU69
AALA135
AASP162
AHIS163
AGLY164
IARG206
AGLN19
AGLY23
ASER24
ACYS25
AGLY61
AGLU63
AGLY68

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL F 1221
ChainResidue
FASN18

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE V65 B 1222
ChainResidue
BGLN19
BGLY23
BSER24
BCYS25
BASN66
BGLY67
BGLY68
BLEU69
FARG206

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL I 1221
ChainResidue
IASN18

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE V65 F 1222
ChainResidue
FGLN19
FGLY23
FCYS25
FGLU63
FCYS65
FASN66
FGLY67
FGLY68
FLEU69
FMET161
FASP162
LARG206

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL L 1221
ChainResidue
LASN18

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE V65 I 1222
ChainResidue
IGLN19
IGLY23
ISER24
ICYS25
ICYS65
IGLY67
IGLY68
IASP162
OARG206

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL O 1221
ChainResidue
OGLY20
OLEU144

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE V65 L 1222
ChainResidue
AARG206
LGLN19
LGLY23
LCYS25
LASN66
LGLY68
LLEU69
LALA135
LASP162

site_idBC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE V65 O 1222
ChainResidue
OGLY23
OCYS25
OASN66
OGLY67
OGLY68
OLEU69
OALA135
OMET161
OASP162
OHIS163
OGLY164

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGqCGSCWAfSA
ChainResidueDetails
AGLN19-ALA30

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. MDHGVLVVGYG
ChainResidueDetails
AMET161-GLY171

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWgeeWGmgGYVkM
ChainResidueDetails
ATYR182-MET201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"evidences":[{"source":"PubMed","id":"9468501","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues66
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37990007","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8HFV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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