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

2ZHR

Crystal structure of BACE1 in complex with OM99-2 at pH 5.0

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 Residues27
DetailsBINDING SITE FOR CHAIN C OF INHIBITOR OM99-2
ChainResidue
AGLY11
AGLU125
AARG128
ATRP197
ATYR198
AASP228
AGLY230
ATHR231
ATHR232
AARG235
AHOH402
AGLN12
AHOH418
AHOH634
CHOH9
CHOH10
CHOH11
CHOH12
CHOH14
CHOH15
ALEU30
AASP32
AGLY34
APRO70
ATYR71
ATHR72
AGLN73

site_idAC2
Number of Residues29
DetailsBINDING SITE FOR CHAIN D OF INHIBITOR OM99-2
ChainResidue
BGLY11
BGLN12
BLEU30
BASP32
BGLY34
BPRO70
BTYR71
BTHR72
BGLN73
BILE110
BGLU125
BARG128
BTYR198
BASP228
BGLY230
BTHR231
BTHR232
BASN233
BARG235
BHOH407
DHOH9
DHOH10
DHOH11
DHOH12
DHOH13
DHOH16
DHOH17
DHOH19
DHOH683

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

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ATHR231
AASP228
ASER35
AASP32

site_idCSA10
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BTHR231
BASP228
BASP32
BTHR33

site_idCSA11
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP32

site_idCSA12
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BASP32

site_idCSA13
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP228

site_idCSA14
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BASP228

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BTHR231
BASP228
BSER35
BASP32

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP228
ASER229
AASP32
ATHR33

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BASP228
BSER229
BASP32
BTHR33

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

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BASP228
BSER35
BASP32

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP228
ASER35
ATYR71
AASP32

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BASP228
BSER35
BTYR71
BASP32

site_idCSA9
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ATHR231
AASP228
AASP32
ATHR33

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon