|
eF-site ID
|
1v7a-A |
PDB Code
|
1v7a |
Chain
|
A |
|
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|
|
Title
|
Crystal structures of adenosine deaminase complexed with potent inhibitors |
Classification
|
HYDROLASE |
Compound
|
adenosine deaminase |
Source
|
ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; |
|
Sequence
|
A: |
TPAFDKPKVELHVHLDGAIKPETILYYGKRRGIALPADTP
EELQNIIGMDKPLTLPDFLAKFDYYMPAIAGCRDAIKRIA
YEFVEMKAKDGVVYVEVRYSPHLLANSKVEPIPWNQAEGD
LTPDEVVSLVNQGLQEGERDFGVKVRSILCCMRHQPSWSS
EVVELCKKYREQTVVAIDLAGDETIEGSSLFPGHVQAYAE
AVKSGVHRTVHAGEVGSANVVKEAVDTLKTERLGHGYHTL
EDTTLYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRF
KNDQVNYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFK
RLNINAAKSSFLPEDEKKELLDLLYKAYR
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
A |
residue |
15 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 400
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
17 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 400
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
214 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 400
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
295 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE ZN A 400
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
17 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE FRC A 1001
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
19 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE FRC A 1001
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
61 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE FRC A 1001
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
62 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE FRC A 1001
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
65 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE FRC A 1001
|
source |
: AC2
|
|
10)
|
chain |
A |
residue |
102 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE FRC A 1001
|
source |
: AC2
|
|
11)
|
chain |
A |
residue |
103 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE FRC A 1001
|
source |
: AC2
|
|
12)
|
chain |
A |
residue |
106 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE FRC A 1001
|
source |
: AC2
|
|
13)
|
chain |
A |
residue |
117 |
type |
|
sequence |
W
|
description |
BINDING SITE FOR RESIDUE FRC A 1001
|
source |
: AC2
|
|
14)
|
chain |
A |
residue |
155 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE FRC A 1001
|
source |
: AC2
|
|
15)
|
chain |
A |
residue |
183 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE FRC A 1001
|
source |
: AC2
|
|
16)
|
chain |
A |
residue |
184 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE FRC A 1001
|
source |
: AC2
|
|
17)
|
chain |
A |
residue |
185 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE FRC A 1001
|
source |
: AC2
|
|
18)
|
chain |
A |
residue |
296 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE FRC A 1001
|
source |
: AC2
|
|
19)
|
chain |
A |
residue |
291-297 |
type |
prosite |
sequence |
SLNTDDP
|
description |
A_DEAMINASE Adenosine and AMP deaminase signature. SLNTDDP
|
source |
prosite : PS00485
|
|
20)
|
chain |
A |
residue |
218 |
type |
ACT_SITE |
sequence |
V
|
description |
Proton donor => ECO:0000250|UniProtKB:P03958
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
21)
|
chain |
A |
residue |
16 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
22)
|
chain |
A |
residue |
18 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
23)
|
chain |
A |
residue |
215 |
type |
BINDING |
sequence |
A
|
description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
24)
|
chain |
A |
residue |
296 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
25)
|
chain |
A |
residue |
20 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
26)
|
chain |
A |
residue |
185 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:16060665, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1WXY
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
27)
|
chain |
A |
residue |
297 |
type |
BINDING |
sequence |
P
|
description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
28)
|
chain |
A |
residue |
59 |
type |
SITE |
sequence |
P
|
description |
Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
29)
|
chain |
A |
residue |
63 |
type |
SITE |
sequence |
A
|
description |
Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
30)
|
chain |
A |
residue |
239 |
type |
SITE |
sequence |
G
|
description |
Important for catalytic activity => ECO:0000250|UniProtKB:P03958
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
31)
|
chain |
A |
residue |
55 |
type |
MOD_RES |
sequence |
P
|
description |
N6-acetyllysine => ECO:0000250|UniProtKB:P00813
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
32)
|
chain |
A |
residue |
233 |
type |
MOD_RES |
sequence |
T
|
description |
N6-acetyllysine => ECO:0000250|UniProtKB:P00813
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
|
|