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1T8L

CRYSTAL STRUCTURE OF THE P1 MET BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0007586biological_processdigestion
A0008236molecular_functionserine-type peptidase activity
A0097180cellular_componentserine protease inhibitor complex
A0097655molecular_functionserpin family protein binding
B0004867molecular_functionserine-type endopeptidase inhibitor activity
C0004252molecular_functionserine-type endopeptidase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0006508biological_processproteolysis
C0007586biological_processdigestion
C0008236molecular_functionserine-type peptidase activity
C0097180cellular_componentserine protease inhibitor complex
C0097655molecular_functionserpin family protein binding
D0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 601
ChainResidue
BPHE4
BGLU7
BARG42
BHOH2001
BHOH2314
DTYR10
DHOH2243

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 602
ChainResidue
BTYR35
BGLY37
BALA40
BHOH671
BHOH682
CLEU97
AHOH660
BARG20

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 603
ChainResidue
BTYR10
BHOH2009
BHOH2255
BHOH2363
BHOH2368
BHOH2376
DPHE4
DGLU7
DARG42

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 B 604
ChainResidue
BPRO2
BASP3
BHOH2011
BHOH2040
BHOH2196
BHOH2403
CTYR171
CTRP172
CSER217
CSER218
CHOH2258

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 605
ChainResidue
ATYR171
ATRP172
ASER217
ASER218
AHOH2003
AHOH2068
AHOH2113
AHOH2429
DPRO2
DASP3

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 606
ChainResidue
ALYS90
AASN91
ASER92
ATRP237
AHOH2325
AHOH2409

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 607
ChainResidue
ALYS93
AASN95
AASN100
AASN101

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 1602
ChainResidue
ALEU97
CHOH1660
DARG20
DTYR35
DGLY37

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 1606
ChainResidue
CLYS90
CASN91
CSER92
CTRP237
CHOH2235
CHOH2287
CHOH2391

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 1607
ChainResidue
CASN95
CASN100
CASN101
CHOH2343
CHOH2517

Functional Information from PROSITE/UniProt
site_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGCrakrnnFksaedC
ChainResidueDetails
BPHE33-CYS51

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC
ChainResidueDetails
AVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SScmGDSGGPLV
ChainResidueDetails
ASER189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Reactive bond for trypsin
ChainResidueDetails
BMET15
DMET15
ASER195
CHIS57
CASP102
CSER195

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CASP102
CSER195
CHIS57

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CASP102
CSER195
CGLY193
CHIS57

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57
AGLY196

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CASP102
CSER195
CHIS57
CGLY196

site_idMCSA1
Number of Residues5
DetailsM-CSA 387
ChainResidueDetails
AHIS57electrostatic stabiliser, proton shuttle (general acid/base)
AASP102modifies pKa
AGLY193electrostatic stabiliser
ASER195covalent catalysis
AGLY196electrostatic stabiliser

site_idMCSA2
Number of Residues5
DetailsM-CSA 387
ChainResidueDetails
CHIS57electrostatic stabiliser, proton shuttle (general acid/base)
CASP102modifies pKa
CGLY193electrostatic stabiliser
CSER195covalent catalysis
CGLY196electrostatic stabiliser

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PDB entries from 2024-05-01

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