Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6UVP

BACE-1 in complex with compound #3

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue QJJ A 401
ChainResidue
ASER10
AILE118
AASP228
ASER229
AGLY230
ATHR232
AHOH527
AHOH697
AGLY11
AGLN12
AGLY13
AASP32
ATYR71
APHE108
AILE110
ATRP115

site_idAC2
Number of Residues15
Detailsbinding site for residue QJM A 402
ChainResidue
AHIS362
AASP363
AGLU364
APHE365
AARG366
ATHR367
AHOH675
AHOH720
AHOH1018
BGLN55
BARG297
BGLU371
BGLY372
BPRO373
BPHE374

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 403
ChainResidue
AASP318
AHOH581
AHOH647
AHOH719
BSER58
BTHR59
BARG61
BARG96

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 404
ChainResidue
AARG50
ATYR51
AGLN53
AHOH865

site_idAC5
Number of Residues7
Detailsbinding site for residue SO4 A 405
ChainResidue
ALYS9
AGLY11
AGLN12
AARG307
ALYS321
AHOH533
AHOH534

site_idAC6
Number of Residues14
Detailsbinding site for residue QJJ B 401
ChainResidue
BSER10
BGLY11
BGLN12
BGLY13
BASP32
BTYR71
BILE110
BILE118
BASP228
BSER229
BGLY230
BTHR232
BHOH597
BHOH832

site_idAC7
Number of Residues13
Detailsbinding site for residue QJJ B 402
ChainResidue
ASER164
AGLU165
AHOH598
BTHR82
BARG96
BASN98
BSER132
BGLU134
BSER139
BLYS142
BHOH531
BHOH735
BHOH772

site_idAC8
Number of Residues14
Detailsbinding site for residue QJJ B 403
ChainResidue
ATHR82
AARG96
AASN98
ASER132
AGLU134
ASER139
ALYS142
AHOH632
BASN162
BSER164
BGLU165
BHOH553
BHOH572
BHOH740

site_idAC9
Number of Residues16
Detailsbinding site for residue QJM B 404
ChainResidue
BASP363
BGLU364
BPHE365
BARG366
BTHR367
BHOH619
BHOH644
BHOH668
AGLN55
AARG297
AGLU371
AGLY372
APRO373
APHE374
AHOH1033
BHIS362

site_idAD1
Number of Residues8
Detailsbinding site for residue GOL B 405
ChainResidue
ASER58
ATHR59
AARG61
AARG96
BASP318
BHOH567
BHOH609
BHOH682

site_idAD2
Number of Residues3
Detailsbinding site for residue GOL B 406
ChainResidue
BARG50
BTYR51
BHOH864

site_idAD3
Number of Residues6
Detailsbinding site for residue SO4 B 407
ChainResidue
ALYS239
BASP106
BLYS107
BHOH514
BHOH533
BHOH616

site_idAD4
Number of Residues7
Detailsbinding site for residue SO4 B 408
ChainResidue
BLYS9
BGLY11
BGLN12
BARG307
BLYS321
BHOH527
BHOH556

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 Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP32
AASP228
BASP32
BASP228

site_idSWS_FT_FI2
Number of Residues14
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
ChainResidueDetails
ALYS65
BLYS218
BLYS224
BLYS238
BLYS239
BLYS246
ALYS214
ALYS218
ALYS224
ALYS238
ALYS239
ALYS246
BLYS65
BLYS214

site_idSWS_FT_FI3
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN92
AASN111
AASN162
AASN293
BASN92
BASN111
BASN162
BASN293

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon