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4GUX

Crystal structure of trypsin:MCoTi-II complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
D0004866molecular_functionendopeptidase inhibitor activity
D0004867molecular_functionserine-type endopeptidase inhibitor activity
D0005576cellular_componentextracellular region
D0006952biological_processdefense response
D0010466biological_processnegative regulation of peptidase activity
D1900004biological_processnegative regulation of serine-type endopeptidase activity
E0004866molecular_functionendopeptidase inhibitor activity
E0004867molecular_functionserine-type endopeptidase inhibitor activity
E0005576cellular_componentextracellular region
E0006952biological_processdefense response
E0010466biological_processnegative regulation of peptidase activity
E1900004biological_processnegative regulation of serine-type endopeptidase activity
F0004866molecular_functionendopeptidase inhibitor activity
F0004867molecular_functionserine-type endopeptidase inhibitor activity
F0005576cellular_componentextracellular region
F0006952biological_processdefense response
F0010466biological_processnegative regulation of peptidase activity
F1900004biological_processnegative regulation of serine-type endopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 301
ChainResidue
AGLU72
AASN74
AVAL77
AGLU82
AHOH544
AHOH548

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 302
ChainResidue
AHOH414
BGLY24
BLYS156
BHOH449
AGLY24
ALYS156
AHOH409

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 301
ChainResidue
BGLU72
BASN74
BVAL77
BGLU82
BHOH564
BHOH565

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT B 302
ChainResidue
BTYR25
BCYS27
BTHR31
BLEU137
BHOH545
BHOH556
BHOH631

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 301
ChainResidue
CGLU72
CASN74
CVAL77
CGLU82
CHOH438
CHOH580

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
AVAL56-CYS61

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPVV
ChainResidueDetails
AASP191-VAL202

site_idPS00286
Number of Residues20
DetailsSQUASH_INHIBITOR Squash family of serine protease inhibitors signature. CPkilkkCrrDsDCpgaCiC
ChainResidueDetails
DCYS8-CYS27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsSITE: Reactive bond
ChainResidueDetails
DLYS10
ELYS10
FLYS10
BHIS60
BASP104
BSER197
CHIS60
CASP104
CSER197

site_idSWS_FT_FI2
Number of Residues6
DetailsCROSSLNK: Cyclopeptide (Ser-Gly) => ECO:0000269|PubMed:10801322
ChainResidueDetails
DSER1
BVAL77
BGLU82
BASP191
BGLN194
BSER197
CGLU72
CASN74
CVAL77
CGLU82
CASP191
DGLY34
CGLN194
CSER197
ESER1
EGLY34
FSER1
FGLY34
ASER197
BGLU72
BASN74

site_idSWS_FT_FI3
Number of Residues6
DetailsCROSSLNK: Isoaspartyl glycine isopeptide (Asp-Gly); alternate => ECO:0000269|PubMed:10801322
ChainResidueDetails
DASP4
DGLY5
EASP4
EGLY5
FASP4
FGLY5

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PDB entries from 2024-09-18

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