eF-site ID 2e1w-A
PDB Code 2e1w
Chain A

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Title Crystal structure 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 FR6 A 1
source : AC2

6) chain A
residue 19
type
sequence D
description BINDING SITE FOR RESIDUE FR6 A 1
source : AC2

7) chain A
residue 61
type
sequence F
description BINDING SITE FOR RESIDUE FR6 A 1
source : AC2

8) chain A
residue 62
type
sequence L
description BINDING SITE FOR RESIDUE FR6 A 1
source : AC2

9) chain A
residue 65
type
sequence F
description BINDING SITE FOR RESIDUE FR6 A 1
source : AC2

10) chain A
residue 106
type
sequence L
description BINDING SITE FOR RESIDUE FR6 A 1
source : AC2

11) chain A
residue 117
type
sequence W
description BINDING SITE FOR RESIDUE FR6 A 1
source : AC2

12) chain A
residue 155
type
sequence M
description BINDING SITE FOR RESIDUE FR6 A 1
source : AC2

13) chain A
residue 157
type
sequence H
description BINDING SITE FOR RESIDUE FR6 A 1
source : AC2

14) chain A
residue 183
type
sequence A
description BINDING SITE FOR RESIDUE FR6 A 1
source : AC2

15) chain A
residue 184
type
sequence G
description BINDING SITE FOR RESIDUE FR6 A 1
source : AC2

16) chain A
residue 185
type
sequence D
description BINDING SITE FOR RESIDUE FR6 A 1
source : AC2

17) chain A
residue 295
type
sequence D
description BINDING SITE FOR RESIDUE FR6 A 1
source : AC2

18) chain A
residue 296
type
sequence D
description BINDING SITE FOR RESIDUE FR6 A 1
source : AC2

19) 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

20) 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

21) 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

22) 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

23) 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

24) 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

25) 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

26) chain A
residue 218
type ACT_SITE
sequence V
description Proton donor => ECO:0000250|UniProtKB:P03958
source Swiss-Prot : SWS_FT_FI1

27) chain A
residue 55
type MOD_RES
sequence P
description N6-acetyllysine => ECO:0000250|UniProtKB:P00813
source Swiss-Prot : SWS_FT_FI9

28) chain A
residue 233
type MOD_RES
sequence T
description N6-acetyllysine => ECO:0000250|UniProtKB:P00813
source Swiss-Prot : SWS_FT_FI9

29) 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

30) 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

31) chain A
residue 239
type SITE
sequence G
description Important for catalytic activity => ECO:0000250|UniProtKB:P03958
source Swiss-Prot : SWS_FT_FI7

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


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