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4LVN

Crystal structure of PfSUB1-prodomain-NIMP.M7 Fab complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI A 701
ChainResidue
AGLU463
AHIS464

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 702
ChainResidue
AGLU338
AASP381
AILE439
AASN442
AILE444
AVAL446

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 703
ChainResidue
AARG396
APHE399
AASP401
AASP408
AHOH891
AGLU392

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 704
ChainResidue
AGLU392
AASP400
AASP402
AASN404
AILE406
AASP409

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NI P 301
ChainResidue
PHIS146

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. ICVIDSGIdynH
ChainResidueDetails
AILE368-HIS379

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVSGiISA
ChainResidueDetails
AHIS428-ALA438

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAaPhVAA
ChainResidueDetails
AGLY604-ALA614

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
BTYR193-HIS199

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Cleavage; by autolysis => ECO:0000269|PubMed:10617661
ChainResidueDetails
PASP217
AHIS428
ASER606

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
PASN171
AILE406
AASP408
AASP409
AILE439
AASN442
AILE444
AVAL446
AASP381
AGLU392
AARG396
APHE399
AASP400
AASP401
AASP402
AASN404

site_idSWS_FT_FI3
Number of Residues5
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN417
AASN488
AASN501
AASN520
AASN603

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PDB entries from 2024-07-31

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