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

1M4H

Crystal Structure of Beta-secretase complexed with Inhibitor OM00-3

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 Residues26
DetailsBINDING SITE FOR CHAIN C OF INHIBITOR OM00-3
ChainResidue
AGLY11
AILE110
AGLU125
AARG128
ATRP197
ATYR198
AASP228
AGLY230
ATHR231
ATHR232
AARG235
AGLN12
AARG307
AHOH398
AHOH419
CHOH15
CHOH52
CHOH85
CHOH225
ALEU30
AASP32
AGLY34
APRO70
ATYR71
ATHR72
AGLN73

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR CHAIN D OF INHIBITOR OM00-3
ChainResidue
BGLY11
BLEU30
BASP32
BGLY34
BPRO70
BTYR71
BTHR72
BGLN73
BILE110
BGLU125
BARG128
BTYR198
BASP228
BGLY230
BTHR231
BTHR232
BARG235
BARG307
BHOH398
BHOH433
BHOH519
DHOH313
DHOH393
DHOH433
DHOH449
DHOH450

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
BLEU80
BPRO276

site_idSWS_FT_FI2
Number of Residues14
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
ChainResidueDetails
ALYS65
BGLN266
BALA272
BTYR286
BLEU287
BGLN294
ALYS214
ALYS218
ALYS224
ALYS238
ALYS239
ALYS246
BSER113
BTRP262

site_idSWS_FT_FI3
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN92
AASN111
AASN162
AASN293
BLEU140
BPHE159
BGLY210
BPHE341

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 Residues2
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP228
AASP32

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BASP228
BASP32

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

222036

PDB entries from 2024-07-03

PDB statisticsPDBj update infoContact PDBjnumon