Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1NPZ

Crystal structures of Cathepsin S inhibitor complexes

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE C1P A 468
ChainResidue
AGLN19
ATYR154
AASN163
AHIS164
ATRP186
AHOH628
BPHE396
BLEU397
AGLY23
ACYS25
ATRP26
AASN67
AGLY68
AGLY69
APHE70
AALA140

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE C1P B 469
ChainResidue
APHE146
ALEU147
BGLN269
BGLY273
BCYS275
BTRP276
BCYS316
BASN317
BGLY318
BGLY319
BPHE320
BALA390
BVAL412
BASN413
BHIS414
BTRP436

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

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VNHGVLVVGYG
ChainResidueDetails
AVAL162-GLY172

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWghnFGeeGYIrM
ChainResidueDetails
ATYR179-MET198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ACYS25
AHIS164
AASN184
BCYS275
BHIS414
BASN434

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AHIS164
ACYS25
AASN184

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BHIS414
BASN434
BCYS275

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AHIS164
AGLN19
ACYS25

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BGLN269
BHIS414
BCYS275

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AHIS164
AGLN19
AASN184

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BGLN269
BHIS414
BASN434

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AHIS164
AGLN19
ACYS25
AASN184

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BGLN269
BHIS414
BASN434
BCYS275

site_idMCSA1
Number of Residues4
DetailsM-CSA 814
ChainResidueDetails
AGLN19electrostatic stabiliser
ACYS25nucleofuge, nucleophile, proton acceptor, proton donor
AHIS164proton acceptor, proton donor
AASN184electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 814
ChainResidueDetails
BGLN269electrostatic stabiliser
BCYS275nucleofuge, nucleophile, proton acceptor, proton donor
BHIS414proton acceptor, proton donor
BASN434electrostatic stabiliser

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon