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1PYT

TERNARY COMPLEX OF PROCARBOXYPEPTIDASE A, PROPROTEINASE E, AND CHYMOTRYPSINOGEN C

Functional Information from GO Data
ChainGOidnamespacecontents
B0004181molecular_functionmetallocarboxypeptidase activity
B0006508biological_processproteolysis
B0008270molecular_functionzinc ion binding
C0004252molecular_functionserine-type endopeptidase activity
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0006508biological_processproteolysis
C0007586biological_processdigestion
D0004252molecular_functionserine-type endopeptidase activity
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0008236molecular_functionserine-type peptidase activity
D0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 650
ChainResidue
CGLU470
CASP472
CVAL475
CGLN477
CGLU480

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 350
ChainResidue
BHIS69
BGLU72
BHIS196
BHOH351

Functional Information from PROSITE/UniProt
site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SAcnGDSGGPLN
ChainResidueDetails
CSER589-ASN600
DSER889-ASN900

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
CVAL453-CYS458
DLEU753-CYS758

site_idPS00132
Number of Residues23
DetailsCARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdlGiHSrEwITQatgvwF
ChainResidueDetails
BPRO60-PHE82

site_idPS00133
Number of Residues11
DetailsCARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLlYPY
ChainResidueDetails
BHIS196-TYR206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000250
ChainResidueDetails
DHIS757
DASP802
DSER895

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
DASN709
BGLU72
BHIS196

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7
ChainResidueDetails
BARG127
BASN144
BSER197
BTYR248

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 171
ChainResidueDetails
BHIS69metal ligand
BGLU72metal ligand
BARG127electrostatic stabiliser, hydrogen bond donor
BHIS196metal ligand
BGLU270covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-04-17

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