eF-site ID 2fdp-C
PDB Code 2fdp
Chain C

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Title Crystal structure of beta-secretase complexed with an amino-ethylene inhibitor
Classification HYDROLASE
Compound Beta-secretase 1
Source Homo sapiens (Human) (BACE1_HUMAN)
Sequence C:  SFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSN
FAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWE
GELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEG
ILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGA
SVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEI
NGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSI
KAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLM
GEVTNQSFRITILPQQYLRPVEDSQDDCYKFAISQSSTGT
VMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVE
GPFVTLDMEDCGYN
Description


Functional site

1) chain C
residue 11
type
sequence G
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

2) chain C
residue 12
type
sequence Q
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

3) chain C
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

4) chain C
residue 32
type
sequence D
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

5) chain C
residue 34
type
sequence G
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

6) chain C
residue 35
type
sequence S
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

7) chain C
residue 70
type
sequence P
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

8) chain C
residue 71
type
sequence Y
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

9) chain C
residue 72
type
sequence T
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

10) chain C
residue 73
type
sequence Q
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

11) chain C
residue 108
type
sequence F
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

12) chain C
residue 126
type
sequence I
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

13) chain C
residue 128
type
sequence R
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

14) chain C
residue 228
type
sequence D
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

15) chain C
residue 230
type
sequence G
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

16) chain C
residue 231
type
sequence T
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

17) chain C
residue 232
type
sequence T
description BINDING SITE FOR RESIDUE FRP C 386
source : AC3

18) chain C
residue 80
type ACT_SITE
sequence L
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
source Swiss-Prot : SWS_FT_FI1

19) chain C
residue 276
type ACT_SITE
sequence P
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
source Swiss-Prot : SWS_FT_FI1

20) chain C
residue 113
type MOD_RES
sequence S
description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
source Swiss-Prot : SWS_FT_FI2

21) chain C
residue 262
type MOD_RES
sequence W
description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
source Swiss-Prot : SWS_FT_FI2

22) chain C
residue 266
type MOD_RES
sequence Q
description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
source Swiss-Prot : SWS_FT_FI2

23) chain C
residue 272
type MOD_RES
sequence A
description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
source Swiss-Prot : SWS_FT_FI2

24) chain C
residue 286
type MOD_RES
sequence Y
description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
source Swiss-Prot : SWS_FT_FI2

25) chain C
residue 287
type MOD_RES
sequence L
description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
source Swiss-Prot : SWS_FT_FI2

26) chain C
residue 294
type MOD_RES
sequence Q
description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
source Swiss-Prot : SWS_FT_FI2

27) chain C
residue 210
type CARBOHYD
sequence G
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI3

28) chain C
residue 341
type CARBOHYD
sequence F
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI3

29) chain C
residue 140
type CARBOHYD
sequence L
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI3


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