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eF-site ID
|
1eve-A |
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PDB Code
|
1eve |
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Chain
|
A |
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click to enlarge
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Title
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THREE DIMENSIONAL STRUCTURE OF THE ANTI-ALZHEIMER DRUG, E2020 (ARICEPT), COMPLEXED WITH ITS TARGET ACETYLCHOLINESTERASE |
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Classification
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SERINE HYDROLASE |
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Compound
|
ACETYLCHOLINESTERASE |
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Source
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ORGANISM_COMMON: Pacific electric ray; ORGANISM_SCIENTIFIC: Torpedo californica; |
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Sequence
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A: |
DHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVG
NMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGS
EMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFY
SGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGS
QEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESA
GGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEG
RRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNV
LPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILL
GVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVP
HANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVI
CPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHG
YEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGN
PNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMC
VFWNQFLPKLLNAT
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Description
|
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Functional site
|
|
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1)
|
chain |
A |
| residue |
200 |
| type |
|
| sequence |
S
|
| description |
CATALYTIC TRIAD.
|
| source |
: CAT
|
|
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2)
|
chain |
A |
| residue |
327 |
| type |
|
| sequence |
E
|
| description |
CATALYTIC TRIAD.
|
| source |
: CAT
|
|
|
3)
|
chain |
A |
| residue |
440 |
| type |
|
| sequence |
H
|
| description |
CATALYTIC TRIAD.
|
| source |
: CAT
|
|
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4)
|
chain |
A |
| residue |
84 |
| type |
|
| sequence |
W
|
| description |
INHIBITOR BINDING SITE.
|
| source |
: IHB
|
|
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5)
|
chain |
A |
| residue |
330 |
| type |
|
| sequence |
F
|
| description |
INHIBITOR BINDING SITE.
|
| source |
: IHB
|
|
|
6)
|
chain |
A |
| residue |
279 |
| type |
|
| sequence |
W
|
| description |
INHIBITOR BINDING SITE.
|
| source |
: IHB
|
|
|
7)
|
chain |
A |
| residue |
187-202 |
| type |
prosite |
| sequence |
FGGDPKTVTIFGESAG
|
| description |
CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpktVtIfGeSAG
|
| source |
prosite : PS00122
|
|
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8)
|
chain |
A |
| residue |
92-102 |
| type |
prosite |
| sequence |
EDCLYLNIWVP
|
| description |
CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIWvP
|
| source |
prosite : PS00941
|
|
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9)
|
chain |
A |
| residue |
200 |
| type |
ACT_SITE |
| sequence |
S
|
| description |
Acyl-ester intermediate
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
10)
|
chain |
A |
| residue |
327 |
| type |
ACT_SITE |
| sequence |
E
|
| description |
Charge relay system
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
11)
|
chain |
A |
| residue |
440 |
| type |
ACT_SITE |
| sequence |
H
|
| description |
Charge relay system
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
12)
|
chain |
A |
| residue |
59 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:16763558
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
|
13)
|
chain |
A |
| residue |
416 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:16763558, ECO:0000269|PubMed:1678899
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
|
14)
|
chain |
A |
| residue |
457 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299
|
| source |
Swiss-Prot : SWS_FT_FI6
|
|
|
15)
|
chain |
A |
| residue |
533 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299
|
| source |
Swiss-Prot : SWS_FT_FI6
|
|
|
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