eF-site ID 1a4l-C
PDB Code 1a4l
Chain 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 C:  TPAFNKPKVELHVHLDGAIKPETILYFGKKRGIALPADTV
EELRNIIGMDKPLSLPGFLAKFDYYMPVIAGCREAIKRIA
YEFVEMKAKEGVVYVEVRYSPHLLANSKVDPMPWNQTEGD
VTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQPSWSL
EVLELCKKYNQKTVVAMDLAGDETIEGSSLFPGHVEAYEG
AVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTI
EDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRF
KNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFK
RLNINAAKSSFLPEEEKKELLERLYREYQ
Description


Functional site

1) chain C
residue 1015
type
sequence H
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC

2) chain C
residue 1017
type
sequence H
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC

3) chain C
residue 1019
type
sequence D
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC

4) chain C
residue 1184
type
sequence G
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC

5) chain C
residue 1214
type
sequence H
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC

6) chain C
residue 1217
type
sequence E
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC

7) chain C
residue 1238
type
sequence H
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC

8) chain C
residue 1295
type
sequence D
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC

9) chain C
residue 1296
type
sequence D
description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE.
source : CIC

10) chain C
residue 1015
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 1400
source : AC2

11) chain C
residue 1017
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 1400
source : AC2

12) chain C
residue 1214
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 1400
source : AC2

13) chain C
residue 1295
type
sequence D
description BINDING SITE FOR RESIDUE ZN C 1400
source : AC2

14) chain C
residue 1015
type
sequence H
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

15) chain C
residue 1017
type
sequence H
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

16) chain C
residue 1019
type
sequence D
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

17) chain C
residue 1058
type
sequence L
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

18) chain C
residue 1061
type
sequence F
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

19) chain C
residue 1062
type
sequence L
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

20) chain C
residue 1065
type
sequence F
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

21) chain C
residue 1102
type
sequence Y
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

22) chain C
residue 1103
type
sequence S
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

23) chain C
residue 1106
type
sequence L
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

24) chain C
residue 1155
type
sequence M
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

25) chain C
residue 1183
type
sequence A
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

26) chain C
residue 1184
type
sequence G
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

27) chain C
residue 1214
type
sequence H
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

28) chain C
residue 1217
type
sequence E
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

29) chain C
residue 1238
type
sequence H
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

30) chain C
residue 1295
type
sequence D
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

31) chain C
residue 1296
type
sequence D
description BINDING SITE FOR RESIDUE DCF C 1353
source : AC7

32) chain C
residue 1015
type catalytic
sequence H
description 376
source MCSA : MCSA3

33) chain C
residue 1017
type catalytic
sequence H
description 376
source MCSA : MCSA3

34) chain C
residue 1214
type catalytic
sequence H
description 376
source MCSA : MCSA3

35) chain C
residue 1217
type catalytic
sequence E
description 376
source MCSA : MCSA3

36) chain C
residue 1238
type catalytic
sequence H
description 376
source MCSA : MCSA3

37) chain C
residue 1295
type catalytic
sequence D
description 376
source MCSA : MCSA3

38) 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

39) 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

40) 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

41) 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

42) 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

43) 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

44) chain C
residue 1054
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P00813
source Swiss-Prot : SWS_FT_FI8

45) chain C
residue 1232
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P00813
source Swiss-Prot : SWS_FT_FI8

46) 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

47) 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

48) 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

49) 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

50) 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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