|
|
1)
|
chain |
B |
residue |
5 |
type |
|
sequence |
I
|
description |
RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
|
source |
: BPT
|
|
2)
|
chain |
B |
residue |
6 |
type |
|
sequence |
A
|
description |
RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
|
source |
: BPT
|
|
3)
|
chain |
B |
residue |
7 |
type |
|
sequence |
A
|
description |
RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
|
source |
: BPT
|
|
4)
|
chain |
B |
residue |
22 |
type |
|
sequence |
W
|
description |
RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
|
source |
: BPT
|
|
5)
|
chain |
B |
residue |
27 |
type |
|
sequence |
D
|
description |
RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
|
source |
: BPT
|
|
6)
|
chain |
B |
residue |
28 |
type |
|
sequence |
L
|
description |
RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
|
source |
: BPT
|
|
7)
|
chain |
B |
residue |
31 |
type |
|
sequence |
F
|
description |
RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
|
source |
: BPT
|
|
8)
|
chain |
B |
residue |
94 |
type |
|
sequence |
I
|
description |
RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
|
source |
: BPT
|
|
9)
|
chain |
B |
residue |
113 |
type |
|
sequence |
T
|
description |
RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
|
source |
: BPT
|
|
10)
|
chain |
B |
residue |
49 |
type |
|
sequence |
S
|
description |
RESIDUES INTERACTING WITH THE N(10) METHYL OF THE METHOTREXATE INHIBITOR
|
source |
: BNM
|
|
11)
|
chain |
B |
residue |
28 |
type |
|
sequence |
L
|
description |
RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR
|
source |
: BAB
|
|
12)
|
chain |
B |
residue |
31 |
type |
|
sequence |
F
|
description |
RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR
|
source |
: BAB
|
|
13)
|
chain |
B |
residue |
50 |
type |
|
sequence |
I
|
description |
RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR
|
source |
: BAB
|
|
14)
|
chain |
B |
residue |
52 |
type |
|
sequence |
R
|
description |
RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR
|
source |
: BAB
|
|
15)
|
chain |
B |
residue |
54 |
type |
|
sequence |
L
|
description |
RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR
|
source |
: BAB
|
|
16)
|
chain |
B |
residue |
28 |
type |
|
sequence |
L
|
description |
RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR
|
source |
: BGL
|
|
17)
|
chain |
B |
residue |
31 |
type |
|
sequence |
F
|
description |
RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR
|
source |
: BGL
|
|
18)
|
chain |
B |
residue |
32 |
type |
|
sequence |
K
|
description |
RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR
|
source |
: BGL
|
|
19)
|
chain |
B |
residue |
54 |
type |
|
sequence |
L
|
description |
RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR
|
source |
: BGL
|
|
20)
|
chain |
B |
residue |
57 |
type |
|
sequence |
R
|
description |
RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR
|
source |
: BGL
|
|
21)
|
chain |
B |
residue |
43 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE CL B 160
|
source |
: AC2
|
|
22)
|
chain |
B |
residue |
46 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE CL B 160
|
source |
: AC2
|
|
23)
|
chain |
B |
residue |
96 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE CL B 160
|
source |
: AC2
|
|
24)
|
chain |
B |
residue |
135 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE CA B 161
|
source |
: AC3
|
|
25)
|
chain |
B |
residue |
5 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE MTX B 162
|
source |
: AC5
|
|
26)
|
chain |
B |
residue |
6 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE MTX B 162
|
source |
: AC5
|
|
27)
|
chain |
B |
residue |
7 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE MTX B 162
|
source |
: AC5
|
|
28)
|
chain |
B |
residue |
27 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE MTX B 162
|
source |
: AC5
|
|
29)
|
chain |
B |
residue |
28 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE MTX B 162
|
source |
: AC5
|
|
30)
|
chain |
B |
residue |
31 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE MTX B 162
|
source |
: AC5
|
|
31)
|
chain |
B |
residue |
32 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE MTX B 162
|
source |
: AC5
|
|
32)
|
chain |
B |
residue |
50 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE MTX B 162
|
source |
: AC5
|
|
33)
|
chain |
B |
residue |
52 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE MTX B 162
|
source |
: AC5
|
|
34)
|
chain |
B |
residue |
54 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE MTX B 162
|
source |
: AC5
|
|
35)
|
chain |
B |
residue |
57 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE MTX B 162
|
source |
: AC5
|
|
36)
|
chain |
B |
residue |
94 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE MTX B 162
|
source |
: AC5
|
|
37)
|
chain |
B |
residue |
100 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE MTX B 162
|
source |
: AC5
|
|
38)
|
chain |
B |
residue |
113 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE MTX B 162
|
source |
: AC5
|
|
39)
|
chain |
B |
residue |
113 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000305|PubMed:9012674
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
40)
|
chain |
B |
residue |
5 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000305|PubMed:9012674
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
41)
|
chain |
B |
residue |
27 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000305|PubMed:9012674
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
42)
|
chain |
B |
residue |
52 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000305|PubMed:9012674
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
43)
|
chain |
B |
residue |
57 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000305|PubMed:9012674
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
44)
|
chain |
B |
residue |
63 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000269|PubMed:19374017
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
45)
|
chain |
B |
residue |
76 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000269|PubMed:19374017
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
46)
|
chain |
B |
residue |
95 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000269|PubMed:19374017
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
47)
|
chain |
B |
residue |
7 |
type |
BINDING |
sequence |
A
|
description |
BINDING => ECO:0000269|PubMed:19374017
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
48)
|
chain |
B |
residue |
13 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000269|PubMed:19374017
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
49)
|
chain |
B |
residue |
45 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000269|PubMed:19374017
|
source |
Swiss-Prot : SWS_FT_FI2
|
|