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eF-site ID
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2ace-A |
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PDB Code
|
2ace |
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Chain
|
A |
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click to enlarge
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Title
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NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO CALIFORNICA |
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Classification
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SERINE HYDROLASE |
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Compound
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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: |
SELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNM
RFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEM
WNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSG
SSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQE
APGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGG
ASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRR
RAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLP
FDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGV
NKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHA
NDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICP
LMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYE
IEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPN
ESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFL
PKLLNAT
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Description
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Functional site
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1)
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chain |
A |
| residue |
200 |
| type |
|
| sequence |
S
|
| description |
CATALYTIC TRIAD.
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| source |
: CAT
|
|
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2)
|
chain |
A |
| residue |
327 |
| type |
|
| sequence |
E
|
| description |
CATALYTIC TRIAD.
|
| source |
: CAT
|
|
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3)
|
chain |
A |
| residue |
440 |
| type |
|
| sequence |
H
|
| description |
CATALYTIC TRIAD.
|
| source |
: CAT
|
|
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4)
|
chain |
A |
| residue |
200 |
| type |
ACT_SITE |
| sequence |
S
|
| description |
Acyl-ester intermediate
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
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5)
|
chain |
A |
| residue |
327 |
| type |
ACT_SITE |
| sequence |
E
|
| description |
Charge relay system
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
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6)
|
chain |
A |
| residue |
440 |
| type |
ACT_SITE |
| sequence |
H
|
| description |
Charge relay system
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
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7)
|
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_FI4
|
|
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8)
|
chain |
A |
| residue |
457 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
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9)
|
chain |
A |
| residue |
533 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
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10)
|
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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11)
|
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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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_FI3
|
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