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3NCL

Crystal Structure of MT-SP1 bound to Benzamidine Phosphonate Inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE CCZ A 500
ChainResidue
AILE36
ASER228
ATRP229
AGLY230
AGLY232
ACYS233
AGLY240
AHOH405
AHOH615
AHIS52
AASP202
ASER203
ACYS204
AGLN205
AGLY206
AASP207
ASER208

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 501
ChainResidue
AARG88
APHE196
ALEU197
AHOH505
AHOH602

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT A 502
ChainResidue
APRO125
AILE126
ASER127
AILE221
AHOH352
AHOH357
AHOH558
AHOH595
AHOH611

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FMT A 503
ChainResidue
ASER127
AALA131
AARG220
AILE221
APHE222
AASP250
AHOH524
AHOH557
AHOH595
AHOH611

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
AVAL48-CYS53

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLS
ChainResidueDetails
AASP202-SER213

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues239
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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