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3BN9

Crystal Structure of MT-SP1 in complex with Fab Inhibitor E2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
D0002250biological_processadaptive immune response
D0002376biological_processimmune system process
D0003823molecular_functionantigen binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005886cellular_componentplasma membrane
D0006955biological_processimmune response
D0016020cellular_componentmembrane
D0016064biological_processimmunoglobulin mediated immune response
D0019814cellular_componentimmunoglobulin complex
D0070062cellular_componentextracellular exosome
D0072562cellular_componentblood microparticle
F0002250biological_processadaptive immune response
F0002376biological_processimmune system process
F0003823molecular_functionantigen binding
F0005576cellular_componentextracellular region
F0005615cellular_componentextracellular space
F0005886cellular_componentplasma membrane
F0006955biological_processimmune response
F0016020cellular_componentmembrane
F0016064biological_processimmunoglobulin mediated immune response
F0019814cellular_componentimmunoglobulin complex
F0070062cellular_componentextracellular exosome
F0072562cellular_componentblood microparticle
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 1
ChainResidue
BHIS91
BLEU233
BPHE234
BTRP237
BHOH381
BHOH420

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 3
ChainResidue
BPRO28
BHIS71
BMET117
BHOH448
BGLY25
BGLU26
BTRP27

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 4
ChainResidue
BPHE184
BLEU185
BSER186
BHOH384
BHOH508

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 6
ChainResidue
BARG230
BPRO232
BLEU233
BHOH367

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 7
ChainResidue
BGLU26
BTRP29
BILE207

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 8
ChainResidue
BALA135
BARG161
BHOH496
BHOH516

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 215
ChainResidue
CGLN37
CLYS39
CLYS42
CLYS45
CHOH337

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO C 216
ChainResidue
CSER65
CGLY66
CASP70
CPHE71
CTHR72

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 217
ChainResidue
BGLY18
CVAL110
CALA111
CALA112

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO D 243
ChainResidue
CTYR96
DGLN100
DASN100
DVAL100
DSER100
DPHE100
DHOH287

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 2
ChainResidue
APHE184
ALEU185
ASER186

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 12
ChainResidue
APRO178
AARG179

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 13
ChainResidue
AHIS91
ATYR101
APHE234
ATRP237

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 E 215
ChainResidue
EGLN37
ELYS39
ELYS42
ELYS45

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO E 216
ChainResidue
EGLN38
EGLY41
ELYS42
FTYR91

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
BVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLS
ChainResidueDetails
BASP189-SER200

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
CTYR192-HIS198
DTYR194-HIS200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system
ChainResidueDetails
BHIS57
BASP102
BSER195
AHIS57
AASP102
ASER195

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN164
AASN164

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57

site_idCSA10
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57

site_idCSA11
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57
BGLY196

site_idCSA12
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57
AGLY196

site_idCSA13
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BSER195
BGLY193
BHIS57
BASP96
BSER214

site_idCSA14
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER195
AGLY193
AHIS57
AASP96
ASER214

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BHIS57

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
AHIS57

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BSER195
BGLY193

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER195
AGLY193

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BSER195
BGLY196

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER195
AGLY196

site_idCSA9
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BGLY193
BHIS57

238268

PDB entries from 2025-07-02

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