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1DLK

CRYSTAL STRUCTURE ANALYSIS OF DELTA-CHYMOTRYPSIN BOUND TO A PEPTIDYL CHLOROMETHYL KETONE INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
B0004252molecular_functionserine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0007586biological_processdigestion
B0008236molecular_functionserine-type peptidase activity
B0097180cellular_componentserine protease inhibitor complex
B0097655molecular_functionserpin family protein binding
D0004252molecular_functionserine-type endopeptidase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0006508biological_processproteolysis
D0007586biological_processdigestion
D0008236molecular_functionserine-type peptidase activity
D0097180cellular_componentserine protease inhibitor complex
D0097655molecular_functionserpin family protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 400
ChainResidue
BLYS90
BHOH504
DGLY59

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR CHAIN E OF PEPTIDIC INHIBITOR
ChainResidue
BGLY193
BSER195
BSER214
BTRP215
BGLY216
BSER217
BHOH453
DSER218
EHOH441
FHOH294
BHIS57
BLEU97
BTHR98
BLYS175
BSER190
BMET192

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR CHAIN F OF PEPTIDIC INHIBITOR
ChainResidue
BMET192
BSER218
DHIS57
DLEU97
DTHR98
DLYS175
DSER190
DGLY193
DSER195
DSER214
DTRP215
DGLY216
DSER217
DHOH275
DHOH290
DHOH386
EHOH441
FHOH294
FHOH383

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC
ChainResidueDetails
BVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SScmGDSGGPLV
ChainResidueDetails
BSER189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system
ChainResidueDetails
BHIS57
BASP102
BSER195
DHIS57
DASP102
DSER195

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DSER195
DHIS57

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BGLY193
BHIS57

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DSER195
DGLY193
DHIS57

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57
BGLY196

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DSER195
DHIS57
DGLY196

site_idMCSA1
Number of Residues5
DetailsM-CSA 387
ChainResidueDetails
BHIS57electrostatic stabiliser, proton shuttle (general acid/base)
BASP102modifies pKa
BGLY193electrostatic stabiliser
BSER195covalent catalysis
BGLY196electrostatic stabiliser

site_idMCSA2
Number of Residues5
DetailsM-CSA 387
ChainResidueDetails
DHIS57electrostatic stabiliser, proton shuttle (general acid/base)
DASP102modifies pKa
DGLY193electrostatic stabiliser
DSER195covalent catalysis
DGLY196electrostatic stabiliser

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PDB entries from 2024-07-17

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