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3R2F

Crystal structure of beta-site app-cleaving enzyme 1 (BACE-WT) complex with BMS-693391 AKA (2S)-2-((3R)-3-acetamido-3-isobutyl-2-oxo-1-pyrrolidinyl)-N-((1S,2R)-1-(3,5-difluorobenzyl)-2-hydroxy-2-((2R,4R)-4-propoxy-2-pyrrolidinyl)ethyl)-4-phenylbutanamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0016020cellular_componentmembrane
D0004190molecular_functionaspartic-type endopeptidase activity
D0006508biological_processproteolysis
D0016020cellular_componentmembrane
E0004190molecular_functionaspartic-type endopeptidase activity
E0006508biological_processproteolysis
E0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE PB0 A 394
ChainResidue
AGLY11
APHE108
AILE110
ATRP115
ATYR198
AASP228
AGLY230
ATHR231
ATHR232
AARG235
AHOH418
ALEU30
AASP32
AGLY34
ASER35
ATYR71
ATHR72
AGLN73
AGLY74

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE PB0 B 394
ChainResidue
BGLY11
BGLN12
BGLY13
BLEU30
BASP32
BGLY34
BSER35
BTYR71
BTHR72
BGLN73
BGLY74
BPHE108
BILE110
BTRP115
BTYR198
BASP228
BGLY230
BTHR231
BTHR232
BARG235
BHOH437

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PB0 D 394
ChainResidue
DGLY11
DGLN12
DGLY13
DASP32
DGLY34
DTYR71
DTHR72
DGLN73
DGLY74
DPHE108
DILE110
DTRP115
DTYR198
DASP228
DGLY230
DTHR231
DTHR232
DARG235

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE PB0 E 394
ChainResidue
EGLY11
EGLN12
EGLY13
ELEU30
EASP32
EGLY34
ESER35
ETYR71
ETHR72
EGLN73
EGLY74
EPHE108
EILE110
ETRP115
ETYR198
EASP228
EGLY230
ETHR231
ETHR232
EARG235
EHOH402

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 Residues1364
DetailsDomain: {"description":"Peptidase A1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"17425515","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19011241","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues16
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2025-10-15

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