|
eF-site ID
|
3dkk-A |
PDB Code
|
3dkk |
Chain
|
A |
|
click to enlarge
|
|
Title
|
Aged Form of Human Butyrylcholinesterase Inhibited by Tabun |
Classification
|
HYDROLASE |
Compound
|
Cholinesterase |
Source
|
(CHLE_HUMAN) |
|
Sequence
|
A: |
DIIIATKNGKVRGMQLTVFGGTVTAFLGIPYAQPPLGRLR
FKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMW
NPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGT
SSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEA
PGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGEXAGAA
SVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNR
TLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPY
GTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVN
KDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVS
EFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPA
LEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEI
EFVFGLPLERRDQYTKAEEILSRSIVKRWANFAKYGNPQE
TQNQSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFW
TSFFPKV
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
A |
residue |
82 |
type |
BINDING |
sequence |
W
|
description |
BINDING => ECO:0007744|PDB:4BDS
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
2)
|
chain |
A |
residue |
438 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0007744|PDB:4BDS
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
3)
|
chain |
A |
residue |
116 |
type |
BINDING |
sequence |
G
|
description |
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
4)
|
chain |
A |
residue |
198 |
type |
ACT_SITE |
sequence |
X
|
description |
Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:12869558
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
5)
|
chain |
A |
residue |
325 |
type |
ACT_SITE |
sequence |
E
|
description |
Charge relay system => ECO:0000269|PubMed:12869558
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
6)
|
chain |
A |
residue |
438 |
type |
ACT_SITE |
sequence |
H
|
description |
Charge relay system => ECO:0000269|PubMed:12869558
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
7)
|
chain |
A |
residue |
198 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphoserine => ECO:0000269|PubMed:22444575
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
8)
|
chain |
A |
residue |
185-200 |
type |
prosite |
sequence |
FGGNPKSVTLFGEXAG
|
description |
CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGnpksVtLfGeSAG
|
source |
prosite : PS00122
|
|
9)
|
chain |
A |
residue |
90-100 |
type |
prosite |
sequence |
EDCLYLNVWIP
|
description |
CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNVWiP
|
source |
prosite : PS00941
|
|
10)
|
chain |
A |
residue |
256 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
11)
|
chain |
A |
residue |
481 |
type |
CARBOHYD |
sequence |
Q
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:3542989
|
source |
Swiss-Prot : SWS_FT_FI11
|
|
12)
|
chain |
A |
residue |
486 |
type |
CARBOHYD |
sequence |
Q
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:3542989
|
source |
Swiss-Prot : SWS_FT_FI11
|
|
13)
|
chain |
A |
residue |
485 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338, ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855
|
source |
Swiss-Prot : SWS_FT_FI12
|
|
14)
|
chain |
A |
residue |
106 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338, ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
15)
|
chain |
A |
residue |
241 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
16)
|
chain |
A |
residue |
17 |
type |
CARBOHYD |
sequence |
Q
|
description |
N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:18203274
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
17)
|
chain |
A |
residue |
455 |
type |
CARBOHYD |
sequence |
Q
|
description |
N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:18203274
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
18)
|
chain |
A |
residue |
57 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338, ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
19)
|
chain |
A |
residue |
341 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338, ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
|
|