eF-site ID 1a4l-A
PDB Code 1a4l
Chain A

click to enlarge
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
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 A
residue 15
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 400
source : AC4

11) chain A
residue 17
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 400
source : AC4

12) chain A
residue 214
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 400
source : AC4

13) chain A
residue 295
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 400
source : AC4

14) chain A
residue 15
type
sequence H
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

15) chain A
residue 17
type
sequence H
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

16) chain A
residue 19
type
sequence D
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

17) chain A
residue 58
type
sequence L
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

18) chain A
residue 61
type
sequence F
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

19) chain A
residue 65
type
sequence F
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

20) chain A
residue 103
type
sequence S
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

21) chain A
residue 106
type
sequence L
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

22) chain A
residue 155
type
sequence M
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

23) chain A
residue 183
type
sequence A
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

24) chain A
residue 184
type
sequence G
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

25) chain A
residue 214
type
sequence H
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

26) chain A
residue 217
type
sequence E
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

27) chain A
residue 238
type
sequence H
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

28) chain A
residue 295
type
sequence D
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

29) chain A
residue 296
type
sequence D
description BINDING SITE FOR RESIDUE DCF A 353
source : AC5

30) chain A
residue 15
type catalytic
sequence H
description 376
source MCSA : MCSA1

31) chain A
residue 17
type catalytic
sequence H
description 376
source MCSA : MCSA1

32) chain A
residue 214
type catalytic
sequence H
description 376
source MCSA : MCSA1

33) chain A
residue 217
type catalytic
sequence E
description 376
source MCSA : MCSA1

34) chain A
residue 238
type catalytic
sequence H
description 376
source MCSA : MCSA1

35) chain A
residue 295
type catalytic
sequence D
description 376
source MCSA : MCSA1

36) chain A
residue 291-297
type prosite
sequence SLNTDDP
description A_DEAMINASE Adenosine and AMP deaminase signature. SLNTDDP
source prosite : PS00485

37) 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

38) 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

39) 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

40) 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

41) 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

42) 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

43) 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

44) 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

45) 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

46) 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

47) 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

48) chain A
residue 54
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P00813
source Swiss-Prot : SWS_FT_FI8

49) chain A
residue 232
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P00813
source Swiss-Prot : SWS_FT_FI8


Display surface

Download
Links