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4NIV

Crystal structure of trypsiligase (K60E/N143H/Y151H/D189K trypsin) trigonal form

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 301
ChainResidue
AGLU70
AASN72
AVAL75
AGLU80
AHOH405
AHOH406

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
AHOH504
AHOH554
AGLU80
AGLN81
APHE82

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
AVAL53-CYS58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS57
AASP102
ASER195

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING:
ChainResidueDetails
AVAL75
AGLU80
ALYS189
AGLN192
ASER195
AGLU70
AASN72

220472

PDB entries from 2024-05-29

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