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3ATK

Crystal structure of trypsin complexed with cycloheptanamine

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
A0008236molecular_functionserine-type peptidase activity
A0046872molecular_functionmetal ion binding
A0097180cellular_componentserine protease inhibitor complex
A0097655molecular_functionserpin family protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1
ChainResidue
AGLU70
AASN72
AVAL75
AGLU80
AHOH268
AHOH306

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DMS A 2
ChainResidue
APHE82
AVAL90
AHIS91
ATYR94
AHOH306
AARG67
AILE73
AASN74

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 3
ChainResidue
ATYR23
ACYS25
ATHR29
AGLN173
AHOH388

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SZ1 A 4
ChainResidue
ASER190
ASER195
AVAL209
ATRP211
AGLY214
AHOH308
AHOH309

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
AVAL54-CYS59

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
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS58
AASP102
ASER195

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING:
ChainResidueDetails
AGLU70
AASN72
AVAL75
AGLU80
AASP189
AGLN192
ASER195

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PDB entries from 2024-07-17

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