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1EJM

CRYSTAL STRUCTURE OF THE BPTI ALA16LEU MUTANT IN COMPLEX WITH BOVINE TRYPSIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0007586biological_processdigestion
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0097180cellular_componentserine protease inhibitor complex
A0097655molecular_functionserpin family protein binding
B0004867molecular_functionserine-type endopeptidase inhibitor activity
C0004175molecular_functionendopeptidase activity
C0004252molecular_functionserine-type endopeptidase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0006508biological_processproteolysis
C0007586biological_processdigestion
C0008233molecular_functionpeptidase activity
C0008236molecular_functionserine-type peptidase activity
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
C0097180cellular_componentserine protease inhibitor complex
C0097655molecular_functionserpin family protein binding
D0004867molecular_functionserine-type endopeptidase inhibitor activity
E0004175molecular_functionendopeptidase activity
E0004252molecular_functionserine-type endopeptidase activity
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0006508biological_processproteolysis
E0007586biological_processdigestion
E0008233molecular_functionpeptidase activity
E0008236molecular_functionserine-type peptidase activity
E0016787molecular_functionhydrolase activity
E0046872molecular_functionmetal ion binding
E0097180cellular_componentserine protease inhibitor complex
E0097655molecular_functionserpin family protein binding
F0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 3601
ChainResidue
CLYS60
CHOH4359
DARG520
DLYS546

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 F 3602
ChainResidue
DARG542
FARG520
FTYR535
FHOH4284

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 3603
ChainResidue
BLYS541
BARG542
BHOH4120
BHOH4539
BHOH4565
BGLU507

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 3604
ChainResidue
DARG520
DTYR535
DHOH4142
FARG542
FHOH4399
FHOH4538

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 F 3605
ChainResidue
DLYS541
DSO43606
DHOH4134
FTYR510
FARG539
FHOH4117

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 3606
ChainResidue
DTYR510
DARG539
FTYR510
FSO43605
FHOH4298

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 3607
ChainResidue
BARG520
BTYR535
BGLY537
BALA540
BHOH4023
BHOH4500

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 E 3608
ChainResidue
EASN100
EASN101
EASN179
EHOH4355

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 3609
ChainResidue
ALYS60
BILE519
BARG520
BLYS546

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 3610
ChainResidue
AASN100
AASN101
AASN179
AHOH4203

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 3611
ChainResidue
DPRO509
DTYR510
DTHR511
DGLY512
DHOH4469

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 3612
ChainResidue
CLYS169
CPRO173
CGLY174
CHOH4048
CHOH4510
CHOH4576

Functional Information from PROSITE/UniProt
site_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGCrakrnnFksaedC
ChainResidueDetails
BPHE533-CYS551

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. DScqGDSGGPVV
ChainResidueDetails
AASP189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsSITE: Reactive bond for trypsin
ChainResidueDetails
BARG515
DARG515
FARG515
CLYS60
CLEU105
CPRO198
ELYS60
ELEU105
EPRO198

site_idSWS_FT_FI2
Number of Residues21
DetailsBINDING:
ChainResidueDetails
AILE73
CGLY78
CILE83
CGLN192
CSER195
CPRO198
EILE73
EVAL75
EGLY78
EILE83
EGLN192
AVAL75
ESER195
EPRO198
AGLY78
AILE83
AGLN192
ASER195
APRO198
CILE73
CVAL75

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PDB entries from 2024-03-27

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