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3UOU

Crystal structure of the Kunitz-type protease inhibitor ShPI-1 Lys13Leu mutant in complex with pancreatic elastase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0046872molecular_functionmetal ion binding
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0019828molecular_functionaspartic-type endopeptidase inhibitor activity
B0042151cellular_componentnematocyst
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AARG62
ASER236
AARG237
AHOH398
BARG11

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
AHOH350
AGLY144
AARG251
ASER253
AALA254

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 3
ChainResidue
AARG75
BARG18
BTYR33
BGLY35

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 4
ChainResidue
AALA115
ATHR193
BARG11

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 56
ChainResidue
BLYS8
BARG11
BHOH59
BHOH72
BHOH101
BHOH178

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 6
ChainResidue
AHOH24
AGLN63
ASER128
AARG237
AHOH279
AHOH306
BLYS8
BVAL9
BGLY10

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 7
ChainResidue
AARG162
AGLN166
AARG207
AHOH372

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 57
ChainResidue
AARG237
BLYS8
BHOH206

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 58
ChainResidue
ATYR46
BPHE16
BPRO17
BARG18

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 267
ChainResidue
ASER186
ASER187
ASER188
BARG50

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 268
ChainResidue
ALYS195
AASN196
ASER197
AHOH337

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 269
ChainResidue
AGLU32
AALA33
AGLN34
AARG35
AARG244

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 5
ChainResidue
ALEU88
AASN89
ALEU167
AALA168
AGLN169
AHOH284
AHOH357

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 270
ChainResidue
AARG80
ATYR97
AHOH326

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 271
ChainResidue
ASER187
AGLY191
ASER192

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. MTAAHC
ChainResidueDetails
AMET67-CYS72

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SGcqGDSGGPLH
ChainResidueDetails
ASER208-HIS219

site_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FiyGGCggngnnFetlhqC
ChainResidueDetails
BPHE31-CYS49

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Reactive bond for trypsin => ECO:0000269|PubMed:22975140
ChainResidueDetails
BLEU13

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:5415110
ChainResidueDetails
AASP119
ASER214

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:7656008, ECO:0007744|PDB:1ELA, ECO:0007744|PDB:1ELB, ECO:0007744|PDB:1ELC
ChainResidueDetails
AGLU85
AASN87
AGLN90
AGLU95

222624

PDB entries from 2024-07-17

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