|
eF-site ID
|
1s2t-B |
PDB Code
|
1s2t |
Chain
|
B |
|
click to enlarge
|
|
Title
|
Crystal Structure Of Apo Phosphoenolpyruvate Mutase |
Classification
|
ISOMERASE |
Compound
|
Phosphoenolpyruvate phosphomutase |
Source
|
Mytilus edulis (Blue mussel) (PEPM_MYTED) |
|
Sequence
|
B: |
KVKKTTQLKQMLNSKDLEFIMEAHNGLSARIVQEAGFKGI
WGSGLSVSAQLGVRDSNEASWTQVVEVLEFMSDASDVPIL
LDADTGYGNFNNARRLVRKLEDRGVAGACLEDKLFPKTNS
LHDGRAQPLADIEEFALKIKACKDSQTDPDFCIVARVEAF
IAGWGLDEALKRAEAYRNAGADAILMHSKKADPSDIEAFM
KAWNNQGPVVIVPTKYYKTPTDHFRDMGVSMVIWANHNLR
ASVSAIQQTTKQIYDDQSLVNVEDKIVSVKEIFRLQRDDE
LVQAEDKYLPK
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
B |
residue |
46 |
type |
catalytic |
sequence |
S
|
description |
271
|
source |
MCSA : MCSA2
|
|
2)
|
chain |
B |
residue |
123 |
type |
catalytic |
sequence |
S
|
description |
271
|
source |
MCSA : MCSA2
|
|
3)
|
chain |
B |
residue |
159 |
type |
catalytic |
sequence |
R
|
description |
271
|
source |
MCSA : MCSA2
|
|
4)
|
chain |
B |
residue |
190 |
type |
catalytic |
sequence |
H
|
description |
271
|
source |
MCSA : MCSA2
|
|
5)
|
chain |
B |
residue |
47 |
type |
catalytic |
sequence |
G
|
description |
271
|
source |
MCSA : MCSA2
|
|
6)
|
chain |
B |
residue |
48 |
type |
catalytic |
sequence |
L
|
description |
271
|
source |
MCSA : MCSA2
|
|
7)
|
chain |
B |
residue |
58 |
type |
catalytic |
sequence |
D
|
description |
271
|
source |
MCSA : MCSA2
|
|
8)
|
chain |
B |
residue |
85 |
type |
catalytic |
sequence |
D
|
description |
271
|
source |
MCSA : MCSA2
|
|
9)
|
chain |
B |
residue |
87 |
type |
catalytic |
sequence |
D
|
description |
271
|
source |
MCSA : MCSA2
|
|
10)
|
chain |
B |
residue |
114 |
type |
catalytic |
sequence |
E
|
description |
271
|
source |
MCSA : MCSA2
|
|
11)
|
chain |
B |
residue |
120 |
type |
catalytic |
sequence |
K
|
description |
271
|
source |
MCSA : MCSA2
|
|
12)
|
chain |
B |
residue |
122 |
type |
catalytic |
sequence |
N
|
description |
271
|
source |
MCSA : MCSA2
|
|
13)
|
chain |
B |
residue |
58 |
type |
ACT_SITE |
sequence |
D
|
description |
Nucleophile => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
14)
|
chain |
B |
residue |
58 |
type |
BINDING |
sequence |
D
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
|
|