|
|
1)
|
chain |
A |
residue |
105 |
type |
|
sequence |
D
|
description |
DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE.
|
source |
: PRA
|
|
2)
|
chain |
A |
residue |
106 |
type |
|
sequence |
D
|
description |
DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE.
|
source |
: PRA
|
|
3)
|
chain |
A |
residue |
107 |
type |
|
sequence |
V
|
description |
DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE.
|
source |
: PRA
|
|
4)
|
chain |
A |
residue |
108 |
type |
|
sequence |
L
|
description |
DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE.
|
source |
: PRA
|
|
5)
|
chain |
A |
residue |
109 |
type |
|
sequence |
Y
|
description |
DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE.
|
source |
: PRA
|
|
6)
|
chain |
A |
residue |
110 |
type |
|
sequence |
T
|
description |
DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE.
|
source |
: PRA
|
|
7)
|
chain |
A |
residue |
111 |
type |
|
sequence |
G
|
description |
DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE.
|
source |
: PRA
|
|
8)
|
chain |
A |
residue |
112 |
type |
|
sequence |
R
|
description |
DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE.
|
source |
: PRA
|
|
9)
|
chain |
A |
residue |
113 |
type |
|
sequence |
T
|
description |
DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE.
|
source |
: PRA
|
|
10)
|
chain |
A |
residue |
40 |
type |
|
sequence |
K
|
description |
DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE.
|
source |
: PRA
|
|
11)
|
chain |
A |
residue |
10 |
type |
|
sequence |
E
|
description |
SM3+ ION BINDING SITE. THE SM3+ ION LIES ON A CRYSTALLOGRAPHIC TWO-FOLD AXIS, AND ISOCTAHEDRALLY COORDINATED BY THE OXYGENS OF THREE AMINO ACID SIDE CHAINS AND THEIR SYMMETRY RELATED ATOMS.
|
source |
: SM1
|
|
12)
|
chain |
A |
residue |
167 |
type |
|
sequence |
D
|
description |
SM3+ ION BINDING SITE. THE SM3+ ION LIES ON A CRYSTALLOGRAPHIC TWO-FOLD AXIS, AND ISOCTAHEDRALLY COORDINATED BY THE OXYGENS OF THREE AMINO ACID SIDE CHAINS AND THEIR SYMMETRY RELATED ATOMS.
|
source |
: SM1
|
|
13)
|
chain |
A |
residue |
173 |
type |
|
sequence |
D
|
description |
SM3+ ION BINDING SITE. THE SM3+ ION LIES ON A CRYSTALLOGRAPHIC TWO-FOLD AXIS, AND ISOCTAHEDRALLY COORDINATED BY THE OXYGENS OF THREE AMINO ACID SIDE CHAINS AND THEIR SYMMETRY RELATED ATOMS.
|
source |
: SM1
|
|
14)
|
chain |
A |
residue |
10 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE SM A 182
|
source |
: AC1
|
|
15)
|
chain |
A |
residue |
10 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE SM A 182
|
source |
: AC1
|
|
16)
|
chain |
A |
residue |
167 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE SM A 182
|
source |
: AC1
|
|
17)
|
chain |
A |
residue |
167 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE SM A 182
|
source |
: AC1
|
|
18)
|
chain |
A |
residue |
173 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE SM A 182
|
source |
: AC1
|
|
19)
|
chain |
A |
residue |
173 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE SM A 182
|
source |
: AC1
|
|
20)
|
chain |
A |
residue |
40 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE SO4 A 184
|
source |
: AC3
|
|
21)
|
chain |
A |
residue |
105 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE SO4 A 184
|
source |
: AC3
|
|
22)
|
chain |
A |
residue |
107 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE SO4 A 184
|
source |
: AC3
|
|
23)
|
chain |
A |
residue |
108 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE SO4 A 184
|
source |
: AC3
|
|
24)
|
chain |
A |
residue |
109 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE SO4 A 184
|
source |
: AC3
|
|
25)
|
chain |
A |
residue |
110 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE SO4 A 184
|
source |
: AC3
|
|
26)
|
chain |
A |
residue |
111 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE SO4 A 184
|
source |
: AC3
|
|
27)
|
chain |
A |
residue |
112 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE SO4 A 184
|
source |
: AC3
|
|
28)
|
chain |
A |
residue |
113 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE SO4 A 184
|
source |
: AC3
|
|
29)
|
chain |
A |
residue |
114 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE SO4 A 184
|
source |
: AC3
|
|
30)
|
chain |
A |
residue |
41 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
31)
|
chain |
A |
residue |
105 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
32)
|
chain |
A |
residue |
138 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
33)
|
chain |
A |
residue |
162 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|