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4MPW

Human beta-tryptase co-crystal structure with [(1,1,3,3-tetramethyldisiloxane-1,3-diyl)di-1-benzofuran-3,5-diyl]bis({4-[3-(aminomethyl)phenyl]piperidin-1-yl}methanone)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0006952biological_processdefense response
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0022617biological_processextracellular matrix disassembly
A0031012cellular_componentextracellular matrix
A0042802molecular_functionidentical protein binding
B0004252molecular_functionserine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006508biological_processproteolysis
B0006952biological_processdefense response
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0016787molecular_functionhydrolase activity
B0022617biological_processextracellular matrix disassembly
B0031012cellular_componentextracellular matrix
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 301
ChainResidue
ATRP42

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGE A 302
ChainResidue
AVAL50
APHE58
ALYS81
AASP82
AALA85
AHOH614

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 303
ChainResidue
AGLN221
AGLY222
ASER224
AHOH466
AHOH554
APHE58
AHIS74

site_idAC4
Number of Residues26
DetailsBINDING SITE FOR RESIDUE 2AJ B 301
ChainResidue
ATHR115
AGLN117
AASP218
ASER219
ACYS220
AGLN221
ASER224
ATRP244
AGLY245
AGLU246
AGLY247
BTHR115
BGLN117
BASP218
BSER219
BCYS220
BGLN221
BSER224
BTRP244
BGLY245
BGLU246
BGLY247
BHOH410
BHOH426
BHOH438
BHOH519

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT B 302
ChainResidue
BPHE58
BHIS74
BGLN221
BGLY222
BSER224
BHOH414
BHOH464

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 303
ChainResidue
BTRP42
BTRP44
BHOH557

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE B 304
ChainResidue
BPHE58
BLYS81
BASP82
BHOH463
BHOH593

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU70-CYS75

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLV
ChainResidueDetails
AASP218-VAL229

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues482
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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