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

1BRA

RELOCATING A NEGATIVE CHARGE IN THE BINDING POCKET OF TRYPSIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0007584biological_processresponse to nutrient
A0007586biological_processdigestion
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0030574biological_processcollagen catabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 302
ChainResidue
AGLU70
AASN72
AVAL75
AGLU77
AGLU80
AHOH261

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BEN A 246
ChainResidue
ASER190
AGLN192
ASER195
AVAL213
ASER214
AGLY216
AGLY219
AASP226
AHOH359
AHOH391

site_idCAT
Number of Residues3
DetailsCATALYTIC TRIAD RESIDUES, CONSERVED IN ALL SERINE PROTEASES OF THE TRYPSIN AND SUBTILISIN STRUCTURAL CLASSES
ChainResidue
AHIS57
AASP102
ASER195

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
AVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. GScqGDSGGPVV
ChainResidueDetails
AGLY189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS57
AASP102
ASER195

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AGLU70
AASN72
AVAL75
AGLU80

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Required for specificity => ECO:0000250
ChainResidueDetails
AGLY189

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon