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3PVK

Secreted aspartic protease 2 in complex with benzamidine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
AASP57
AGLU324
AIMD4002
AIMD4003

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BEN A 2001
ChainResidue
ABEN3001
AMPD4001
ATYR84
AASP86
AGLY220
ATHR221
AILE305

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BEN A 3001
ChainResidue
AASP32
AGLY34
ASER35
ATYR84
ALEU216
AASP218
AHOH375
ABEN2001

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 4001
ChainResidue
AILE30
AASP32
ASER88
AGLY220
ABEN2001

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IMD A 4002
ChainResidue
AASP57
AASP322
AGLU324
AZN1001
AIMD4003

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE IMD A 4003
ChainResidue
ATHR55
AASP57
AGLN61
AGLU324
AHOH606
AZN1001
AIMD4002

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIVDTGSSDLWV
ChainResidueDetails
AVAL29-VAL40
AVAL215-LEU226

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP32
AASP218

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0CY29
ChainResidueDetails
AASP32
AGLY85
AASP191
AASP214
AASP218

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN257
AASN265

222926

PDB entries from 2024-07-24

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