eF-site ID 2zjj-A
PDB Code 2zjj
Chain A

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Title Crystal structure of the human BACE1 catalytic domain in complex with 4-(4-fluoro-benzyl)-piperazine-2-carboxylic acid (2-mercapto-ethyl)-amide
Classification HYDROLASE
Compound Beta-secretase 1
Source Homo sapiens (Human) (BACE1_HUMAN)
Sequence A:  GSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSS
NFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGAW
AGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWE
GILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCG
AGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEIN
GQDLKMDCKEYNYDKSIVDSGCTNLRLPKKVFEAAVKSIK
AASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMG
EVTNQSFRITILPQQYLRPVEDDCYKFAISQSSTGTVMGA
VIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFV
TLDMEDCGYN
Description


Functional site

1) chain A
residue 11
type
sequence G
description BINDING SITE FOR RESIDUE F1J A 449
source : AC1

2) chain A
residue 12
type
sequence Q
description BINDING SITE FOR RESIDUE F1J A 449
source : AC1

3) chain A
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE F1J A 449
source : AC1

4) chain A
residue 30
type
sequence L
description BINDING SITE FOR RESIDUE F1J A 449
source : AC1

5) chain A
residue 71
type
sequence Y
description BINDING SITE FOR RESIDUE F1J A 449
source : AC1

6) chain A
residue 72
type
sequence T
description BINDING SITE FOR RESIDUE F1J A 449
source : AC1

7) chain A
residue 73
type
sequence Q
description BINDING SITE FOR RESIDUE F1J A 449
source : AC1

8) chain A
residue 108
type
sequence F
description BINDING SITE FOR RESIDUE F1J A 449
source : AC1

9) chain A
residue 230
type
sequence G
description BINDING SITE FOR RESIDUE F1J A 449
source : AC1

10) chain A
residue 231
type
sequence C
description BINDING SITE FOR RESIDUE F1J A 449
source : AC1

11) chain A
residue 232
type
sequence T
description BINDING SITE FOR RESIDUE F1J A 449
source : AC1

12) chain A
residue 29-40
type prosite
sequence ILVDTGSSNFAV
description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
source prosite : PS00141

13) chain A
residue 32
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
source Swiss-Prot : SWS_FT_FI1

14) chain A
residue 228
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
source Swiss-Prot : SWS_FT_FI1

15) chain A
residue 65
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
source Swiss-Prot : SWS_FT_FI2

16) chain A
residue 214
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
source Swiss-Prot : SWS_FT_FI2

17) chain A
residue 218
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
source Swiss-Prot : SWS_FT_FI2

18) chain A
residue 224
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
source Swiss-Prot : SWS_FT_FI2

19) chain A
residue 238
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
source Swiss-Prot : SWS_FT_FI2

20) chain A
residue 239
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
source Swiss-Prot : SWS_FT_FI2

21) chain A
residue 246
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
source Swiss-Prot : SWS_FT_FI2

22) chain A
residue 92
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI3

23) chain A
residue 111
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI3

24) chain A
residue 293
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI3


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