|
eF-site ID
|
1azy-A |
PDB Code
|
1azy |
Chain
|
A |
|
click to enlarge
|
|
Title
|
STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE |
Classification
|
GLYCOSYLTRANSFERASE |
Compound
|
THYMIDINE PHOSPHORYLASE |
Source
|
ORGANISM_SCIENTIFIC: Escherichia coli; |
|
Sequence
|
A: |
LFLAQEIIRKKRDGHALSDEEIRFFINGIRDNTISEGQIA
ALAMTIFFHDMTMPERVSLTMAMRDSGTVLDWKSLHLNGP
IVDKHSTGGVGDVTSLMLGPMVAACGGYIPMISGRGLGHT
GGTLDKLESIPGFDIFPDDNRFREIIKDVGVAIIGQTSSL
APADKRFYATRDITATVDSIPLITASILAKKLAEGLDALV
MDVKVGSGAFMPTYELSEALAEAIVGVANGAGVRTTALLT
DMNQVLASSAGNAVEVREAVQFLTGEYRNPRLFDVTMALC
VEMLISGKLAKDDAEARAKLQAVLDNGKAAEVFGRMVAAQ
KGPTDFVENYAKYLPTAMLTKAVYADTEGFVSEMDTRALG
MAVVAMGGGRRQASDTIDYSVGFTDMARLGDQVDGQRPLA
VIHAKDENNWQEAAKAVKAAIKLADKAPESTPTVYRRISE
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
A |
residue |
84 |
type |
|
sequence |
K
|
description |
PHOSPHATE BINDING SITE.
|
source |
: P4A
|
|
2)
|
chain |
A |
residue |
85 |
type |
|
sequence |
H
|
description |
PHOSPHATE BINDING SITE.
|
source |
: P4A
|
|
3)
|
chain |
A |
residue |
86 |
type |
|
sequence |
S
|
description |
PHOSPHATE BINDING SITE.
|
source |
: P4A
|
|
4)
|
chain |
A |
residue |
95 |
type |
|
sequence |
S
|
description |
PHOSPHATE BINDING SITE.
|
source |
: P4A
|
|
5)
|
chain |
A |
residue |
113 |
type |
|
sequence |
S
|
description |
PHOSPHATE BINDING SITE.
|
source |
: P4A
|
|
6)
|
chain |
A |
residue |
123 |
type |
|
sequence |
T
|
description |
PHOSPHATE BINDING SITE.
|
source |
: P4A
|
|
7)
|
chain |
A |
residue |
171 |
type |
|
sequence |
R
|
description |
THYMIDINE BINDING SITE.
|
source |
: TYA
|
|
8)
|
chain |
A |
residue |
186 |
type |
|
sequence |
S
|
description |
THYMIDINE BINDING SITE.
|
source |
: TYA
|
|
9)
|
chain |
A |
residue |
190 |
type |
|
sequence |
K
|
description |
THYMIDINE BINDING SITE.
|
source |
: TYA
|
|
10)
|
chain |
A |
residue |
83 |
type |
catalytic |
sequence |
D
|
description |
413
|
source |
MCSA : MCSA1
|
|
11)
|
chain |
A |
residue |
84 |
type |
catalytic |
sequence |
K
|
description |
413
|
source |
MCSA : MCSA1
|
|
12)
|
chain |
A |
residue |
85 |
type |
catalytic |
sequence |
H
|
description |
413
|
source |
MCSA : MCSA1
|
|
13)
|
chain |
A |
residue |
86 |
type |
catalytic |
sequence |
S
|
description |
413
|
source |
MCSA : MCSA1
|
|
14)
|
chain |
A |
residue |
123 |
type |
catalytic |
sequence |
T
|
description |
413
|
source |
MCSA : MCSA1
|
|
15)
|
chain |
A |
residue |
171 |
type |
catalytic |
sequence |
R
|
description |
413
|
source |
MCSA : MCSA1
|
|
16)
|
chain |
A |
residue |
186 |
type |
catalytic |
sequence |
S
|
description |
413
|
source |
MCSA : MCSA1
|
|
17)
|
chain |
A |
residue |
190 |
type |
catalytic |
sequence |
K
|
description |
413
|
source |
MCSA : MCSA1
|
|
18)
|
chain |
A |
residue |
191 |
type |
catalytic |
sequence |
K
|
description |
413
|
source |
MCSA : MCSA1
|
|
19)
|
chain |
A |
residue |
113-128 |
type |
prosite |
sequence |
SGRGLGHTGGTLDKLE
|
description |
THYMID_PHOSPHORYLASE Thymidine and pyrimidine-nucleoside phosphorylases signature. SGRGLghTGGTlDkLE
|
source |
prosite : PS00647
|
|
|
|