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eF-site ID
|
1vfl-A |
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PDB Code
|
1vfl |
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Chain
|
A |
|
click to enlarge
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Title
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Adenosine deaminase |
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Classification
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HYDROLASE |
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Compound
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Adenosine deaminase |
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Source
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ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; |
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Sequence
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A: |
TPAFDKPKVELHVHLDGAIKPETILYYGKRRGIALPADTP
EELQNIIGMDKPLTLPDFLAKFDYYMPAIAGCRDAIKRIA
YEFVEMKAKDGVVYVEVRYSPHLLANSKVEPIPWNQAEGD
LTPDEVVSLVNQGLQEGERDFGVKVRSILCCMRHQPSWSS
EVVELCKKYREQTVVAIDLAGDETIEGSSLFPGHVQAYAE
AVKSGVHRTVHAGEVGSANVVKEAVDTLKTERLGHGYHTL
EDTTLYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRF
KNDQVNYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFK
RLNINAAKSSFLPEDEKKELLDLLYKAYR
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Description
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Functional site
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|
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1)
|
chain |
A |
| residue |
12 |
| type |
|
| sequence |
H
|
| description |
BINDING SITE FOR RESIDUE ZN A 501
|
| source |
: AC1
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2)
|
chain |
A |
| residue |
14 |
| type |
|
| sequence |
H
|
| description |
BINDING SITE FOR RESIDUE ZN A 501
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| source |
: AC1
|
|
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3)
|
chain |
A |
| residue |
211 |
| type |
|
| sequence |
H
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| description |
BINDING SITE FOR RESIDUE ZN A 501
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| source |
: AC1
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|
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4)
|
chain |
A |
| residue |
292 |
| type |
|
| sequence |
D
|
| description |
BINDING SITE FOR RESIDUE ZN A 501
|
| source |
: AC1
|
|
|
5)
|
chain |
A |
| residue |
52 |
| type |
MOD_RES |
| sequence |
P
|
| description |
N6-acetyllysine => ECO:0000250|UniProtKB:P00813
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| source |
Swiss-Prot : SWS_FT_FI9
|
|
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6)
|
chain |
A |
| residue |
230 |
| type |
MOD_RES |
| sequence |
T
|
| description |
N6-acetyllysine => ECO:0000250|UniProtKB:P00813
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| source |
Swiss-Prot : SWS_FT_FI9
|
|
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7)
|
chain |
A |
| residue |
215 |
| type |
ACT_SITE |
| sequence |
V
|
| description |
Proton donor => ECO:0000250|UniProtKB:P03958
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
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8)
|
chain |
A |
| residue |
13 |
| 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
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| source |
Swiss-Prot : SWS_FT_FI2
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|
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9)
|
chain |
A |
| residue |
15 |
| 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
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|
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10)
|
chain |
A |
| residue |
212 |
| 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
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|
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11)
|
chain |
A |
| residue |
293 |
| 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
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|
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12)
|
chain |
A |
| residue |
17 |
| 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
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| source |
Swiss-Prot : SWS_FT_FI3
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|
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13)
|
chain |
A |
| residue |
182 |
| 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
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|
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14)
|
chain |
A |
| residue |
294 |
| 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
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| source |
Swiss-Prot : SWS_FT_FI5
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15)
|
chain |
A |
| residue |
60 |
| type |
SITE |
| sequence |
A
|
| description |
Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813
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| source |
Swiss-Prot : SWS_FT_FI6
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|
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16)
|
chain |
A |
| residue |
56 |
| 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
|
|
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17)
|
chain |
A |
| residue |
236 |
| type |
SITE |
| sequence |
G
|
| description |
Important for catalytic activity => ECO:0000250|UniProtKB:P03958
|
| source |
Swiss-Prot : SWS_FT_FI7
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|
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18)
|
chain |
A |
| residue |
288-294 |
| type |
prosite |
| sequence |
SLNTDDP
|
| description |
A_DEAMINASE Adenosine and AMP deaminase signature. SLNTDDP
|
| source |
prosite : PS00485
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