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2PH6

Crystal Structure of Human Beta Secretase Complexed with inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 386
ChainResidue
AARG96
AASN98
AGLU134
ASER139
AGLN143

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE 712 A 401
ChainResidue
ALEU30
AASP32
AGLY34
ATYR71
ATHR72
AGLN73
AASP228
ASER229
AGLY230
ATHR231
ATHR232
AASN233
AARG235
AARG307
ASER325
AALA335
AHOH506
AHOH595
AGLY11
AGLN12
AGLY13
ATYR14

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
ChainResidueDetails
AILE29-VAL40

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"17425515","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19011241","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP32

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP228

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ATHR231
AASP228
ASER35
AASP32

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP228
ASER229
AASP32
ATHR33

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP228
ASER35
AASP32

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP228
ASER35
ATYR71
AASP32

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ATHR231
AASP228
AASP32
ATHR33

239492

PDB entries from 2025-07-30

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