eF-site ID 1a4l-AC
PDB Code 1a4l
Chain A, C

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Title ADA STRUCTURE COMPLEXED WITH DEOXYCOFORMYCIN AT PH 7.0
Classification HYDROLASE
Compound ADENOSINE DEAMINASE
Source Mus musculus (Mouse) (ADA_MOUSE)
Sequence A:  TPAFNKPKVELHVHLDGAIKPETILYFGKKRGIALPADTV
EELRNIIGMDKPLSLPGFLAKFDYYMPVIAGCREAIKRIA
YEFVEMKAKEGVVYVEVRYSPHLLANSKVDPMPWNQTEGD
VTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQPSWSL
EVLELCKKYNQKTVVAMDLAGDETIEGSSLFPGHVEAYEG
AVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTI
EDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRF
KNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFK
RLNINAAKSSFLPEEEKKELLERLYREYQ
C:  TPAFNKPKVELHVHLDGAIKPETILYFGKKRGIALPADTV
EELRNIIGMDKPLSLPGFLAKFDYYMPVIAGCREAIKRIA
YEFVEMKAKEGVVYVEVRYSPHLLANSKVDPMPWNQTEGD
VTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQPSWSL
EVLELCKKYNQKTVVAMDLAGDETIEGSSLFPGHVEAYEG
AVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTI
EDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRF
KNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFK
RLNINAAKSSFLPEEEKKELLERLYREYQ
Description


Functional site
1) chain A
residue 15
type
sequence H
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIA
2) chain A
residue 17
type
sequence H
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIA
3) chain A
residue 19
type
sequence D
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIA
4) chain A
residue 184
type
sequence G
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIA
5) chain A
residue 214
type
sequence H
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIA
6) chain A
residue 217
type
sequence E
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIA
7) chain A
residue 238
type
sequence H
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIA
8) chain A
residue 295
type
sequence D
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIA
9) chain A
residue 296
type
sequence D
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIA
10) chain C
residue 1015
type
sequence H
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC
11) chain C
residue 1017
type
sequence H
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC
12) chain C
residue 1019
type
sequence D
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC
13) chain C
residue 1184
type
sequence G
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC
14) chain C
residue 1214
type
sequence H
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC
15) chain C
residue 1217
type
sequence E
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC
16) chain C
residue 1238
type
sequence H
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC
17) chain C
residue 1295
type
sequence D
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC
18) chain C
residue 1296
type
sequence D
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC
19) chain C
residue 1015
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 1400
source : AC2
20) chain C
residue 1017
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 1400
source : AC2
21) chain C
residue 1214
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 1400
source : AC2
22) chain C
residue 1295
type
sequence D
description BINDING SITE FOR RESIDUE ZN C 1400
source : AC2
23) chain A
residue 15
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 400
source : AC4
24) chain A
residue 17
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 400
source : AC4
25) chain A
residue 214
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 400
source : AC4
26) chain A
residue 295
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 400
source : AC4
27) chain A
residue 15
type
sequence H
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
28) chain A
residue 17
type
sequence H
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
29) chain A
residue 19
type
sequence D
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
30) chain A
residue 58
type
sequence L
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
31) chain A
residue 61
type
sequence F
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
32) chain A
residue 65
type
sequence F
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
33) chain A
residue 103
type
sequence S
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
34) chain A
residue 106
type
sequence L
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
35) chain A
residue 155
type
sequence M
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
36) chain A
residue 183
type
sequence A
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
37) chain A
residue 184
type
sequence G
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
38) chain A
residue 214
type
sequence H
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
39) chain A
residue 217
type
sequence E
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
40) chain A
residue 238
type
sequence H
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
41) chain A
residue 295
type
sequence D
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
42) chain A
residue 296
type
sequence D
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5
43) chain C
residue 1015
type
sequence H
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
44) chain C
residue 1017
type
sequence H
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
45) chain C
residue 1019
type
sequence D
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
46) chain C
residue 1058
type
sequence L
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
47) chain C
residue 1061
type
sequence F
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
48) chain C
residue 1062
type
sequence L
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
49) chain C
residue 1065
type
sequence F
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
50) chain C
residue 1102
type
sequence Y
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
51) chain C
residue 1103
type
sequence S
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
52) chain C
residue 1106
type
sequence L
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
53) chain C
residue 1155
type
sequence M
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
54) chain C
residue 1183
type
sequence A
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
55) chain C
residue 1184
type
sequence G
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
56) chain C
residue 1214
type
sequence H
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
57) chain C
residue 1217
type
sequence E
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
58) chain C
residue 1238
type
sequence H
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
59) chain C
residue 1295
type
sequence D
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
60) chain C
residue 1296
type
sequence D
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7
61) chain A
residue 15
type catalytic
sequence H
description 376
source MCSA : MCSA1
62) chain A
residue 17
type catalytic
sequence H
description 376
source MCSA : MCSA1
63) chain A
residue 214
type catalytic
sequence H
description 376
source MCSA : MCSA1
64) chain A
residue 217
type catalytic
sequence E
description 376
source MCSA : MCSA1
65) chain A
residue 238
type catalytic
sequence H
description 376
source MCSA : MCSA1
66) chain A
residue 295
type catalytic
sequence D
description 376
source MCSA : MCSA1
67) chain C
residue 1015
type catalytic
sequence H
description 376
source MCSA : MCSA3
68) chain C
residue 1017
type catalytic
sequence H
description 376
source MCSA : MCSA3
69) chain C
residue 1214
type catalytic
sequence H
description 376
source MCSA : MCSA3
70) chain C
residue 1217
type catalytic
sequence E
description 376
source MCSA : MCSA3
71) chain C
residue 1238
type catalytic
sequence H
description 376
source MCSA : MCSA3
72) chain C
residue 1295
type catalytic
sequence D
description 376
source MCSA : MCSA3
73) chain A
residue 15
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA
source Swiss-Prot : SWS_FT_FI2
74) chain C
residue 1017
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA
source Swiss-Prot : SWS_FT_FI2
75) chain C
residue 1214
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA
source Swiss-Prot : SWS_FT_FI2
76) chain C
residue 1295
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA
source Swiss-Prot : SWS_FT_FI2
77) chain A
residue 17
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA
source Swiss-Prot : SWS_FT_FI2
78) chain A
residue 214
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA
source Swiss-Prot : SWS_FT_FI2
79) chain A
residue 295
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA
source Swiss-Prot : SWS_FT_FI2
80) chain C
residue 1015
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA
source Swiss-Prot : SWS_FT_FI2
81) chain A
residue 19
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX
source Swiss-Prot : SWS_FT_FI3
82) chain C
residue 1019
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX
source Swiss-Prot : SWS_FT_FI3
83) chain A
residue 184
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA
source Swiss-Prot : SWS_FT_FI4
84) chain C
residue 1184
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA
source Swiss-Prot : SWS_FT_FI4
85) chain A
residue 54
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P00813
source Swiss-Prot : SWS_FT_FI8
86) chain A
residue 232
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P00813
source Swiss-Prot : SWS_FT_FI8
87) chain C
residue 1054
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P00813
source Swiss-Prot : SWS_FT_FI8
88) chain C
residue 1232
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P00813
source Swiss-Prot : SWS_FT_FI8
89) chain A
residue 291-297
type prosite
sequence SLNTDDP
description A_DEAMINASE Adenosine and AMP deaminase signature. SLNTDDP
source prosite : PS00485
90) chain A
residue 296
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1UIP
source Swiss-Prot : SWS_FT_FI5
91) chain C
residue 1296
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1UIP
source Swiss-Prot : SWS_FT_FI5
92) chain A
residue 217
type ACT_SITE
sequence E
description Proton donor => ECO:0000305|PubMed:8634299, ECO:0000305|PubMed:9622483
source Swiss-Prot : SWS_FT_FI1
93) chain C
residue 1217
type ACT_SITE
sequence E
description Proton donor => ECO:0000305|PubMed:8634299, ECO:0000305|PubMed:9622483
source Swiss-Prot : SWS_FT_FI1
94) chain A
residue 58
type SITE
sequence L
description Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813
source Swiss-Prot : SWS_FT_FI6
95) chain A
residue 62
type SITE
sequence L
description Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813
source Swiss-Prot : SWS_FT_FI6
96) chain C
residue 1058
type SITE
sequence L
description Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813
source Swiss-Prot : SWS_FT_FI6
97) chain C
residue 1062
type SITE
sequence L
description Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813
source Swiss-Prot : SWS_FT_FI6
98) chain A
residue 238
type SITE
sequence H
description Important for catalytic activity => ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483
source Swiss-Prot : SWS_FT_FI7
99) chain C
residue 1238
type SITE
sequence H
description Important for catalytic activity => ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483
source Swiss-Prot : SWS_FT_FI7

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