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1OXG

Crystal structure of a complex formed between organic solvent treated bovine alpha-chymotrypsin and its autocatalytically produced highly potent 14-residue peptide at 2.2 resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0007586biological_processdigestion
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0097180cellular_componentserine protease inhibitor complex
A0097655molecular_functionserpin family protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1001
ChainResidue
ASER115
AGLN116
AASN167
ATHR222
ASER223
AHOH1037
AHOH1049
AHOH1135

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1002
ChainResidue
AASP178
BILE1
BVAL2
BASN3
ALYS177

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1003
ChainResidue
AASN95
AASN100
AASN101
AHOH1059

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1004
ChainResidue
ATHR61
ATHR62
AHOH1093
AHOH1150

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 1005
ChainResidue
AHOH1077

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 1006
ChainResidue
ALYS175
ALYS175
BGLY10
BGLY10
BSER11
BSER11
BHOH149
BHOH149
BHOH225
BHOH225

Functional Information from PROSITE/UniProt
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 Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
AHIS57

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER195
AGLY196

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER195
AGLY193

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57

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
AASP102
ASER195
AGLY193
AHIS57

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

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PDB entries from 2025-07-16

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