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5V0N

BACE1 in complex with inhibitor 5g

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0016020cellular_componentmembrane
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
C0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue SO4 A 401
ChainResidue
AARG235
ASER327
ASER328
AHOH502
AHOH565

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 402
ChainResidue
AHOH555
AHOH635
APHE47
ALYS107
AHOH503
AHOH507

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 403
ChainResidue
AARG96
AGLU134
AHOH511

site_idAC4
Number of Residues17
Detailsbinding site for residue 8W4 A 404
ChainResidue
AGLY11
ALEU30
AASP32
AGLY34
ASER35
ATYR71
ATHR72
AGLN73
AILE126
ATYR198
AASP228
AGLY230
ATHR231
ATHR232
AASN233
AARG235
ASER325

site_idAC5
Number of Residues3
Detailsbinding site for residue URE A 405
ChainResidue
AARG307
ALYS321
AHOH522

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 B 401
ChainResidue
BARG235
BGLN326
BSER327
BSER328
BHOH502

site_idAC7
Number of Residues6
Detailsbinding site for residue SO4 B 402
ChainResidue
BARG96
BALA97
BASN98
BGLU134
BHOH528
BHOH568

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 B 403
ChainResidue
BARG50
BTYR51
BGLN53
BHOH508

site_idAC9
Number of Residues4
Detailsbinding site for residue SO4 B 404
ChainResidue
BASN293
BLEU377
BHOH526
CARG205

site_idAD1
Number of Residues7
Detailsbinding site for residue GOL B 405
ChainResidue
BARG205
BVAL375
BTHR376
BHOH560
CTHR292
CASP378
CHOH539

site_idAD2
Number of Residues15
Detailsbinding site for residue 8W4 B 406
ChainResidue
BASP32
BGLY34
BSER35
BTYR71
BTHR72
BGLN73
BILE126
BTYR198
BASP228
BGLY230
BTHR231
BTHR232
BASN233
BARG235
BSER325

site_idAD3
Number of Residues2
Detailsbinding site for residue URE B 407
ChainResidue
BGLU219
BTYR222

site_idAD4
Number of Residues4
Detailsbinding site for residue SO4 C 401
ChainResidue
CVAL3
CGLN153
CHOH526
CHOH540

site_idAD5
Number of Residues3
Detailsbinding site for residue SO4 C 402
ChainResidue
BGLU371
CASN293
CGLN294

site_idAD6
Number of Residues5
Detailsbinding site for residue SO4 C 403
ChainResidue
CARG96
CALA97
CASN98
CGLU134
CHOH514

site_idAD7
Number of Residues2
Detailsbinding site for residue SO4 C 404
ChainResidue
CARG61
CHOH536

site_idAD8
Number of Residues16
Detailsbinding site for residue 8W4 C 405
ChainResidue
CTYR198
CASP228
CGLY230
CTHR231
CTHR232
CASN233
CARG235
CSER325
CGLY11
CASP32
CGLY34
CSER35
CTYR71
CTHR72
CGLN73
CILE126

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 Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP32
AASP228
BASP32
BASP228
CASP32
CASP228

site_idSWS_FT_FI2
Number of Residues21
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
ChainResidueDetails
ALYS65
BLYS218
BLYS224
BLYS238
BLYS239
BLYS246
CLYS65
CLYS214
CLYS218
CLYS224
CLYS238
ALYS214
CLYS239
CLYS246
ALYS218
ALYS224
ALYS238
ALYS239
ALYS246
BLYS65
BLYS214

site_idSWS_FT_FI3
Number of Residues12
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN92
CASN111
CASN162
CASN293
AASN111
AASN162
AASN293
BASN92
BASN111
BASN162
BASN293
CASN92

223532

PDB entries from 2024-08-07

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