eF-site ID 2va9-AB
PDB Code 2va9
Chain A, B

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Title Structure of native TcAChE after a 9 seconds annealing to room temperature during the first 5 seconds of which laser irradiation at 266nm took place
Classification HYDROLASE
Compound ACETYLCHOLINESTERASE
Source ORGANISM_COMMON: PACIFIC ELECTRIC RAY; ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
Sequence A:  SELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNM
RFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEM
WNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSG
SSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQE
APGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGG
ASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRR
RAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLP
FDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGV
NKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHA
NDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICP
LMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYE
IEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPN
EPSKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQF
LPKLLNAT
B:  SELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNM
RFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEM
WNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSG
SSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQE
APGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGG
ASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRR
RAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLP
FDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGV
NKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHA
NDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICP
LMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYE
IEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPN
EPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVF
WNQFLPKLLNAT
Description


Functional site

1) chain A
residue 187-202
type prosite
sequence FGGDPKTVTIFGESAG
description CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpktVtIfGeSAG
source prosite : PS00122

2) chain A
residue 92-102
type prosite
sequence EDCLYLNIWVP
description CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIWvP
source prosite : PS00941

3) chain A
residue 200
type ACT_SITE
sequence S
description Acyl-ester intermediate
source Swiss-Prot : SWS_FT_FI1

4) chain B
residue 200
type ACT_SITE
sequence S
description Acyl-ester intermediate
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 327
type ACT_SITE
sequence E
description Charge relay system
source Swiss-Prot : SWS_FT_FI2

6) chain A
residue 440
type ACT_SITE
sequence H
description Charge relay system
source Swiss-Prot : SWS_FT_FI2

7) chain B
residue 327
type ACT_SITE
sequence E
description Charge relay system
source Swiss-Prot : SWS_FT_FI2

8) chain B
residue 440
type ACT_SITE
sequence H
description Charge relay system
source Swiss-Prot : SWS_FT_FI2

9) 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

10) chain B
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

11) 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

12) chain B
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

13) chain A
residue 457
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299
source Swiss-Prot : SWS_FT_FI5

14) chain A
residue 533
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299
source Swiss-Prot : SWS_FT_FI5

15) chain B
residue 457
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299
source Swiss-Prot : SWS_FT_FI5

16) chain B
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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