Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6JD8

Structure of a proline specific mutant of human cathepsin L

Functional Information from GO Data
ChainGOidnamespacecontents
A0001968molecular_functionfibronectin binding
A0002250biological_processadaptive immune response
A0004197molecular_functioncysteine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005518molecular_functioncollagen binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005764cellular_componentlysosome
A0005771cellular_componentmultivesicular body
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0016324cellular_componentapical plasma membrane
A0016540biological_processprotein autoprocessing
A0016787molecular_functionhydrolase activity
A0019064biological_processfusion of virus membrane with host plasma membrane
A0019065biological_processreceptor-mediated endocytosis of virus by host cell
A0019882biological_processantigen processing and presentation
A0019886biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II
A0030574biological_processcollagen catabolic process
A0031012cellular_componentextracellular matrix
A0031410cellular_componentcytoplasmic vesicle
A0031638biological_processzymogen activation
A0034230biological_processenkephalin processing
A0036021cellular_componentendolysosome lumen
A0039654biological_processfusion of virus membrane with host endosome membrane
A0042393molecular_functionhistone binding
A0042583cellular_componentchromaffin granule
A0043202cellular_componentlysosomal lumen
A0043373biological_processCD4-positive, alpha-beta T cell lineage commitment
A0043394molecular_functionproteoglycan binding
A0046718biological_processsymbiont entry into host cell
A0048002biological_processantigen processing and presentation of peptide antigen
A0051603biological_processobsolete proteolysis involved in protein catabolic process
A0060309biological_processelastin catabolic process
A0070062cellular_componentextracellular exosome
A0071682cellular_componentendocytic vesicle lumen
A0071888biological_processmacrophage apoptotic process
A0097067biological_processcellular response to thyroid hormone stimulus
A0097655molecular_functionserpin family protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue GOL A 401
ChainResidue
APHE135
AGLY139
AARG140
ALEU141
AHOH507
AHOH536
AHOH601

site_idAC2
Number of Residues3
Detailsbinding site for residue EOH A 402
ChainResidue
AHOH524
AASP300
AARG302

site_idAC3
Number of Residues7
Detailsbinding site for residue EOH A 403
ChainResidue
AGLU159
AASN162
AGLY163
ATYR165
ASER270
ATHR271
AHOH572

site_idAC4
Number of Residues6
Detailsbinding site for residue EOH A 404
ChainResidue
AGLU51
ALYS53
ALEU93
AVAL202
AHOH591
AHOH597

site_idAC5
Number of Residues1
Detailsbinding site for residue EOH A 405
ChainResidue
ALYS87

site_idAC6
Number of Residues4
Detailsbinding site for residue EOH A 406
ChainResidue
AGLY116
AGLN117
AALA189
AEDO415

site_idAC7
Number of Residues8
Detailsbinding site for residue EOH A 407
ChainResidue
AGLY154
AASN158
AGLU159
AGLY160
AGLU191
AHOH537
AHOH546
AHOH586

site_idAC8
Number of Residues3
Detailsbinding site for residue EOH A 408
ChainResidue
AASN38
ASER68
AGLU237

site_idAC9
Number of Residues5
Detailsbinding site for residue EOH A 409
ChainResidue
ALYS87
ACYS194
ATYR196
ATHR206
AHOH532

site_idAD1
Number of Residues3
Detailsbinding site for residue EOH A 410
ChainResidue
ATHR1
ATHR3
APHE4

site_idAD2
Number of Residues2
Detailsbinding site for residue EOH A 411
ChainResidue
AGLU28
AARG32

site_idAD3
Number of Residues4
Detailsbinding site for residue EOH A 412
ChainResidue
ALYS113
ASER143
AGLU182
AHOH559

site_idAD4
Number of Residues6
Detailsbinding site for residue EOH A 413
ChainResidue
APHE124
AGLU146
AGLU182
ATYR187
AHOH602
AHOH692

site_idAD5
Number of Residues5
Detailsbinding site for residue PEG A 414
ChainResidue
AASP205
ATHR206
AHOH542
AHOH547
AHOH624

site_idAD6
Number of Residues4
Detailsbinding site for residue EDO A 415
ChainResidue
ATYR187
AGLN214
AEOH406
AHOH584

site_idAD7
Number of Residues14
Detailsbinding site for residue PGE A 416
ChainResidue
AVAL74
AMET75
AASN76
AGLY77
APHE78
AGLN115
AGLY119
ASER120
ASER121
AGLY163
AGLY164
AASP258
AHIS259
ATHR271

Functional Information from PROSITE/UniProt
site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. LDHAVLVVGYG
ChainResidueDetails
ALEU257-GLY267

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWgeeWGmgGYVkM
ChainResidueDetails
ATYR278-MET297

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"9468501","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37990007","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8HFV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Cleavage; by autolysis","evidences":[{"source":"PubMed","id":"9468501","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
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

250835

PDB entries from 2026-03-18

PDB statisticsPDBj update infoContact PDBjnumon