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5XW1

Crystal Structure of Porcine pancreatic trypsin with tripeptide inhibitor, PRN, at pH10

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 301
ChainResidue
AGLU60
AASN62
AVAL65
AGLU67
AGLU70
AHOH440

site_idAC2
Number of Residues3
Detailsbinding site for residue MPD B 301
ChainResidue
BGLN163
BTRP201
BHOH426

site_idAC3
Number of Residues7
Detailsbinding site for residue MPD B 302
ChainResidue
APRO114
AARG115
AHOH416
BTHR165
BVAL221
BHOH418
BHOH420

site_idAC4
Number of Residues5
Detailsbinding site for residue MPD B 303
ChainResidue
AGLU123
BVAL190
BCYS191
BASN192
BGLY193

Functional Information from PROSITE/UniProt
site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPVV
ChainResidueDetails
BASP179-VAL190

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
AVAL44-CYS49

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Charge relay system
ChainResidueDetails
BSER185
AASP92

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Required for specificity => ECO:0000250
ChainResidueDetails
AVAL65
AGLU70
BASP179
AASN62

221051

PDB entries from 2024-06-12

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