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6JD0

Structure of mutant human cathepsin L, engineered for GAG binding

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
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0006955biological_processimmune response
A0008234molecular_functioncysteine-type peptidase activity
A0008656molecular_functioncysteine-type endopeptidase activator activity involved in apoptotic process
A0016324cellular_componentapical plasma membrane
A0016540biological_processprotein autoprocessing
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
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
A0043231cellular_componentintracellular membrane-bounded organelle
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_processproteolysis involved in protein catabolic process
A0060309biological_processelastin catabolic process
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
A0071682cellular_componentendocytic vesicle lumen
A0071888biological_processmacrophage apoptotic process
A0097067biological_processcellular response to thyroid hormone stimulus
A0097655molecular_functionserpin family protein binding
A2001235biological_processpositive regulation of apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue GOL A 401
ChainResidue
AHIS45
AHIS54
AHOH535

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL A 402
ChainResidue
AGOL404
AHOH514
AHOH521
ALEU22
AGLY24
ATRP103
AARG136
AALA223
ATHR224

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 403
ChainResidue
AVAL88
APHE89
AGLN90

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL A 404
ChainResidue
ATYR95
APRO98
ATRP103
AALA223
AGOL402
AHOH514
AHOH551
AHOH576

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 405
ChainResidue
AARG140
AILE142
AVAL202
AGOL410

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 406
ChainResidue
AVAL109
ATHR110
APRO111
ATYR294
APO4426
AHOH537
AHOH555

site_idAC7
Number of Residues11
Detailsbinding site for residue GOL A 407
ChainResidue
AASN80
AARG81
ALYS82
AARG84
ATYR165
AASP167
ATYR168
AHOH502
AHOH509
AHOH546
AHOH573

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL A 408
ChainResidue
AGLU183
ASER184
APRO186
APGE441

site_idAC9
Number of Residues3
Detailsbinding site for residue GOL A 409
ChainResidue
APRO98
AARG99
ASER100

site_idAD1
Number of Residues6
Detailsbinding site for residue GOL A 410
ChainResidue
AGLY177
AGLY178
ASER201
AALA203
AASN204
AGOL405

site_idAD2
Number of Residues7
Detailsbinding site for residue GOL A 411
ChainResidue
AARG104
ATHR190
AGLU191
AASN291
ALYS296
APGE443
AHOH569

site_idAD3
Number of Residues6
Detailsbinding site for residue GOL A 412
ChainResidue
AGLY24
AMET25
AASN26
AGLU27
AARG136
AHOH517

site_idAD4
Number of Residues3
Detailsbinding site for residue GOL A 413
ChainResidue
ALYS14
AARG302
APGE445

site_idAD5
Number of Residues5
Detailsbinding site for residue GOL A 414
ChainResidue
AGLN47
AGLU91
APRO92
ALEU93
APHE94

site_idAD6
Number of Residues5
Detailsbinding site for residue CL A 415
ChainResidue
ASER68
AGLU69
ANA418
APOL438
AHOH639

site_idAD7
Number of Residues2
Detailsbinding site for residue CL A 416
ChainResidue
ALYS105
AGLN117

site_idAD8
Number of Residues2
Detailsbinding site for residue CL A 417
ChainResidue
APRO212
ALYS213

site_idAD9
Number of Residues6
Detailsbinding site for residue NA A 418
ChainResidue
ATHR67
AGLU69
AGLY107
APHE135
ALEU141
ACL415

site_idAE1
Number of Residues5
Detailsbinding site for residue NA A 419
ChainResidue
AVAL112
ALYS113
AGLY286
APO4428
APOL435

site_idAE2
Number of Residues5
Detailsbinding site for residue NA A 420
ChainResidue
ASER193
ACYS194
AGLU244
ANA422
APO4424

site_idAE3
Number of Residues3
Detailsbinding site for residue NA A 421
ChainResidue
AGLU43
AARG50
APO4423

site_idAE4
Number of Residues4
Detailsbinding site for residue NA A 422
ChainResidue
ATHR57
ASER193
AGLU244
ANA420

site_idAE5
Number of Residues5
Detailsbinding site for residue PO4 A 423
ChainResidue
AASN46
AARG50
ANA421
APO4425
APOL431

site_idAE6
Number of Residues5
Detailsbinding site for residue PO4 A 424
ChainResidue
AASP151
ALYS243
ANA420
AHOH533
AHOH602

site_idAE7
Number of Residues2
Detailsbinding site for residue PO4 A 425
ChainResidue
AARG50
APO4423

site_idAE8
Number of Residues6
Detailsbinding site for residue PO4 A 426
ChainResidue
AARG72
ACYS161
AASN162
AGOL406
AHOH524
AHOH542

site_idAE9
Number of Residues3
Detailsbinding site for residue PO4 A 427
ChainResidue
APHE248
AARG301
AARG302

site_idAF1
Number of Residues6
Detailsbinding site for residue PO4 A 428
ChainResidue
AASN114
AGLY286
AGLU287
AGLU288
ANA419
AHOH568

site_idAF2
Number of Residues2
Detailsbinding site for residue PO4 A 429
ChainResidue
AARG84
ALYS213

site_idAF3
Number of Residues4
Detailsbinding site for residue PO4 A 430
ChainResidue
ATHR138
AGLY139
AARG140
AHOH637

site_idAF4
Number of Residues5
Detailsbinding site for residue POL A 431
ChainResidue
AALA59
AMET60
APO4423
AHOH520
AHOH581

site_idAF5
Number of Residues5
Detailsbinding site for residue POL A 432
ChainResidue
AVAL34
AASN38
AGLU237
AHOH592
AHOH625

site_idAF6
Number of Residues3
Detailsbinding site for residue POL A 433
ChainResidue
AGLU255
AASN303
ASER309

site_idAF7
Number of Residues1
Detailsbinding site for residue POL A 434
ChainResidue
ALEU240

site_idAF8
Number of Residues3
Detailsbinding site for residue POL A 435
ChainResidue
ALYS113
AASN114
ANA419

site_idAF9
Number of Residues4
Detailsbinding site for residue POL A 436
ChainResidue
ALEU22
APHE94
ATYR95
AGLU96

site_idAG1
Number of Residues6
Detailsbinding site for residue POL A 437
ChainResidue
AGLY86
ALYS87
AGLN171
AGLN174
AGLY207
APHE208

site_idAG2
Number of Residues4
Detailsbinding site for residue POL A 438
ChainResidue
AGLY139
AARG140
ALEU141
ACL415

site_idAG3
Number of Residues9
Detailsbinding site for residue POL A 439
ChainResidue
AVAL74
AMET75
AASN76
AGLN115
AGLY119
ASER120
ASER121
AASP258
AHIS259

site_idAG4
Number of Residues2
Detailsbinding site for residue POL A 440
ChainResidue
ASER143
AHOH552

site_idAG5
Number of Residues5
Detailsbinding site for residue PGE A 441
ChainResidue
ASER184
ATYR185
ALYS195
AASN197
AGOL408

site_idAG6
Number of Residues4
Detailsbinding site for residue PGE A 442
ChainResidue
ASER55
AASN275
ALYS277
AARG301

site_idAG7
Number of Residues10
Detailsbinding site for residue PGE A 443
ChainResidue
AGLU192
ASER193
ALYS195
ATYR242
AGLU244
AGLY245
AGLU269
AASN291
ALYS296
AGOL411

site_idAG8
Number of Residues7
Detailsbinding site for residue PGE A 444
ChainResidue
ALEU2
ATHR3
APHE4
AHIS6
AARG99
AEDO451
AHOH512

site_idAG9
Number of Residues5
Detailsbinding site for residue PGE A 445
ChainResidue
ALYS82
ALYS85
AGLN156
AARG302
AGOL413

site_idAH1
Number of Residues4
Detailsbinding site for residue PGE A 446
ChainResidue
AASN114
AGLY116
AGLU188
AEDO450

site_idAH2
Number of Residues4
Detailsbinding site for residue EOH A 447
ChainResidue
AASP233
AASP251
ASER253
AHOH532

site_idAH3
Number of Residues5
Detailsbinding site for residue EOH A 448
ChainResidue
ALYS16
AARG21
AHOH522
AHOH565
AHOH656

site_idAH4
Number of Residues8
Detailsbinding site for residue EOH A 449
ChainResidue
AVAL150
AASP151
AGLY154
AASN158
AGLU191
AHOH533
AHOH602
AHOH610

site_idAH5
Number of Residues7
Detailsbinding site for residue EDO A 450
ChainResidue
ASER100
AVAL101
ATYR266
AGLY267
APHE268
ATYR278
APGE446

site_idAH6
Number of Residues5
Detailsbinding site for residue EDO A 451
ChainResidue
APHE4
ATRP12
AGLU28
AARG32
APGE444

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. YWLvKNSWgeeWGnkGYVkM
ChainResidueDetails
ATYR278-MET297

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:9468501
ChainResidueDetails
ASER121

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AHIS259
AASN283

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Cleavage; by autolysis => ECO:0000269|PubMed:9468501
ChainResidueDetails
APHE89
AGLN90
ATYR95
AGLU96

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN204

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PDB entries from 2024-07-24

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