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6PZ4

co-crystal structure of BACE with inhibitor AM-6494

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue IOD A 501
ChainResidue
ASER166

site_idAC2
Number of Residues1
Detailsbinding site for residue IOD A 502
ChainResidue
ALYS168

site_idAC3
Number of Residues2
Detailsbinding site for residue IOD A 503
ChainResidue
AHOH876
AHOH876

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL A 504
ChainResidue
AHOH645
AHOH810
AHOH815
AARG111
ATYR112
AGLN114
ASER248
AHOH611

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 505
ChainResidue
AGLY127
ATYR129
ACYS330
ATHR375
AHOH602

site_idAC6
Number of Residues16
Detailsbinding site for residue P6J A 506
ChainResidue
ALYS70
AGLY72
AGLN73
AGLY74
ATYR75
AASP93
AGLY95
ATYR132
ALYS168
APHE169
AASP289
ASER290
AGLY291
ATHR293
AALA396
AHOH782

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
ChainResidueDetails
AILE90-VAL101

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

243911

PDB entries from 2025-10-29

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