|
|
1)
|
chain |
A |
residue |
185 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE DTP A 716
|
source |
: AC2
|
|
2)
|
chain |
A |
residue |
186 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE DTP A 716
|
source |
: AC2
|
|
3)
|
chain |
A |
residue |
187 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE DTP A 716
|
source |
: AC2
|
|
4)
|
chain |
A |
residue |
202 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE DTP A 716
|
source |
: AC2
|
|
5)
|
chain |
A |
residue |
215 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE DTP A 716
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
221 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE DTP A 716
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
222 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE DTP A 716
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
244 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE DTP A 716
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
246 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE DTP A 716
|
source |
: AC2
|
|
10)
|
chain |
A |
residue |
387 |
type |
ACT_SITE |
sequence |
L
|
description |
Proton acceptor => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
11)
|
chain |
A |
residue |
391 |
type |
ACT_SITE |
sequence |
I
|
description |
Proton acceptor => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
12)
|
chain |
A |
residue |
389 |
type |
ACT_SITE |
sequence |
S
|
description |
Cysteine radical intermediate => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
13)
|
chain |
A |
residue |
162 |
type |
BINDING |
sequence |
P
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
14)
|
chain |
A |
residue |
178 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
15)
|
chain |
A |
residue |
207 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
16)
|
chain |
A |
residue |
387 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
17)
|
chain |
A |
residue |
589 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
18)
|
chain |
A |
residue |
179 |
type |
SITE |
sequence |
F
|
description |
Important for hydrogen atom transfer => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
19)
|
chain |
A |
residue |
416 |
type |
SITE |
sequence |
N
|
description |
Important for hydrogen atom transfer => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
20)
|
chain |
A |
residue |
186 |
type |
SITE |
sequence |
N
|
description |
Allosteric effector binding
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
21)
|
chain |
A |
residue |
216 |
type |
SITE |
sequence |
E
|
description |
Allosteric effector binding
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
22)
|
chain |
A |
residue |
223 |
type |
SITE |
sequence |
R
|
description |
Allosteric effector binding
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
23)
|
chain |
A |
residue |
566-588 |
type |
prosite |
sequence |
WLKLRDDVMRYGIYNQNLQAVPP
|
description |
RIBORED_LARGE Ribonucleotide reductase large subunit signature. WlkLrddvmryGIYNqnlQAvpP
|
source |
prosite : PS00089
|
|
24)
|
chain |
A |
residue |
693 |
type |
SITE |
sequence |
Y
|
description |
Important for electron transfer => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
25)
|
chain |
A |
residue |
694 |
type |
SITE |
sequence |
I
|
description |
Important for electron transfer => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI6
|
|