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3V7T

Crystal Structure of Human Beta-Tryptase Complexed with a Synthetic Inhibitor with a Tropanylamide Scaffold

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0031012cellular_componentextracellular matrix
B0004252molecular_functionserine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0016787molecular_functionhydrolase activity
B0031012cellular_componentextracellular matrix
C0004252molecular_functionserine-type endopeptidase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0008236molecular_functionserine-type peptidase activity
C0016787molecular_functionhydrolase activity
C0031012cellular_componentextracellular matrix
D0004252molecular_functionserine-type endopeptidase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0008236molecular_functionserine-type peptidase activity
D0016787molecular_functionhydrolase activity
D0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 0GX A 301
ChainResidue
AGLN102
AGLY232
ACO3302
AHOH427
AHOH454
CPRO63
CTYR99
CHOH434
AASP203
ASER204
ACYS205
AGLN206
ASER209
AVAL227
ATRP229
AGLY230

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CO3 A 302
ChainResidue
APHE43
AHIS59
AGLN206
AGLY207
ASER209
A0GX301
AHOH426
AHOH469
AHOH512

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 0GX B 301
ChainResidue
BGLN102
BASP203
BSER204
BCYS205
BGLN206
BSER209
BVAL227
BTRP229
BGLY230
BGLY232
BCO3302
BHOH415
BHOH462
DPRO63
DTYR99

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CO3 B 302
ChainResidue
BPHE43
BHIS59
BGLN206
BGLY207
BSER209
B0GX301
BHOH432
BHOH475

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 0GX C 301
ChainResidue
APRO63
ATYR99
CGLN102
CASP203
CSER204
CCYS205
CGLN206
CSER209
CVAL227
CTRP229
CGLY230
CGLY232
CHOH417
CHOH460
CHOH469

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 0GX D 301
ChainResidue
BPRO63
BTYR99
DGLN102
DASP203
DSER204
DCYS205
DGLN206
DSER209
DVAL227
DTRP229
DGLY230
DGLY232
DCYS233

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU55-CYS60

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLV
ChainResidueDetails
AASP203-VAL214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues12
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P21845","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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