Home Research COVID-19 Services Publications People Teaching Job Opening News Forum Lab Only
Online Services

I-TASSER I-TASSER-MTD C-I-TASSER CR-I-TASSER QUARK C-QUARK LOMETS MUSTER CEthreader SEGMER DeepFold DeepFoldRNA FoldDesign COFACTOR COACH MetaGO TripletGO IonCom FG-MD ModRefiner REMO DEMO DEMO-EM SPRING COTH Threpp PEPPI BSpred ANGLOR EDock BSP-SLIM SAXSTER FUpred ThreaDom ThreaDomEx EvoDesign BindProf BindProfX SSIPe GPCR-I-TASSER MAGELLAN ResQ STRUM DAMpred

TM-score TM-align US-align MM-align RNA-align NW-align LS-align EDTSurf MVP MVP-Fit SPICKER HAAD PSSpred 3DRobot MR-REX I-TASSER-MR SVMSEQ NeBcon ResPRE TripletRes DeepPotential WDL-RF ATPbind DockRMSD DeepMSA FASPR EM-Refiner GPU-I-TASSER

BioLiP E. coli GLASS GPCR-HGmod GPCR-RD GPCR-EXP Tara-3D TM-fold DECOYS POTENTIAL RW/RWplus EvoEF HPSF THE-DB ADDRESS Alpaca-Antibody CASP7 CASP8 CASP9 CASP10 CASP11 CASP12 CASP13 CASP14

BioLiP

Structure of PDB 1nb5 Chain C Binding Site BS01

Receptor Information
>1nb5 Chain C (length=220) Species: 9823 (Sus scrofa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YPPSMDWRKKGNFVSPVKNQGSCGSCWTFSTTGALESAVAIATGKMLSLA
EQQLVDCAQNFNNHGCQGGLPSQAFEYIRYNKGIMGEDTYPYKGQDDHCK
FQPDKAIAFVKDVANITMNDEEAMVEAVALYNPVSFAFEVTNDFLMYRKG
IYSSTSCHKTPDKVNHAVLAVGYGEENGIPYWIVKNSWGPQWGMNGYFLI
ERGKNMCGLAACASYPIPLV
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1nb5 Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases
Resolution2.4 Å
Binding residue
(original residue number in PDB)
N59 H61 S69 Q70 N112 V157 C205 S207
Binding residue
(residue number reindexed from 1)
N62 H64 S72 Q73 N115 V164 C212 S214
Enzymatic activity
Catalytic site (original residue number in PDB) Q19 C25 T31 H159
Catalytic site (residue number reindexed from 1) Q20 C26 T32 H166
Enzyme Commision number 3.4.22.16: cathepsin H.
Gene Ontology
Molecular Function
GO:0008234 cysteine-type peptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1nb5, PDBe:1nb5, PDBj:1nb5
PDBsum1nb5
PubMed12581647
UniProtO46427|CATH_PIG Pro-cathepsin H (Gene Name=CTSH)

[Back to BioLiP]

zhanglabzhanggroup.org | +65-6601-1241 | Computing 1, 13 Computing Drive, Singapore 117417