eF-site ID 1ra5-A
PDB Code 1ra5
Chain A

click to enlarge
Title Bacterial cytosine deaminase D314A mutant bound to 5-fluoro-4-(S)-hydroxyl-3,4-dihydropyrimidine.
Classification HYDROLASE
Compound Cytosine deaminase
Source Escherichia coli (strain K12) (CODA_ECOLI)
Sequence A:  ALQTIINARLPGEEGLWQIHLQDGKISAIDAQSGVMPITE
NSLDAEQGLVIPPFVEPHIHLDTTQTAGQPNWNQSGTLFE
GIERWAERKALLTHDDVKQRAWQTLKWQIANGIQHVRTHV
DVSDATLTALKAMLEVKQEVAPWIDLQIVAFPQEGILSYP
NGEALLEEALRLGADVVGAIPHFEFTREYGVESLHKTFAL
AQKYDRLIDVHCDEIDDEQSRFVETVAALAHHEGMGARVT
ASHTTAMHSYNGAYTSRLFRLLKMSGINFVANPLVNIHLQ
GRFDTYPKRRGITRVKEMLESGINVCFGHDAVFDPWYPLG
TANMLQVLHMGLHVCQLMGYGQINDGLNLITHHSARTLNL
QDYGIAAGNSANLIILPAENGFDALRRQVPVRYSVRGGKV
IASTQPAQTTVYLEQPEAIDYKR
Description


Functional site

1) chain A
residue 61
type
sequence H
description BINDING SITE FOR RESIDUE FE A 500
source : AC1

2) chain A
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE FE A 500
source : AC1

3) chain A
residue 214
type
sequence H
description BINDING SITE FOR RESIDUE FE A 500
source : AC1

4) chain A
residue 246
type
sequence H
description BINDING SITE FOR RESIDUE FE A 500
source : AC1

5) chain A
residue 313
type
sequence D
description BINDING SITE FOR RESIDUE FE A 500
source : AC1

6) chain A
residue 61
type
sequence H
description BINDING SITE FOR RESIDUE FPY A 501
source : AC2

7) chain A
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE FPY A 501
source : AC2

8) chain A
residue 81
type
sequence L
description BINDING SITE FOR RESIDUE FPY A 501
source : AC2

9) chain A
residue 154
type
sequence F
description BINDING SITE FOR RESIDUE FPY A 501
source : AC2

10) chain A
residue 156
type
sequence Q
description BINDING SITE FOR RESIDUE FPY A 501
source : AC2

11) chain A
residue 214
type
sequence H
description BINDING SITE FOR RESIDUE FPY A 501
source : AC2

12) chain A
residue 217
type
sequence E
description BINDING SITE FOR RESIDUE FPY A 501
source : AC2

13) chain A
residue 246
type
sequence H
description BINDING SITE FOR RESIDUE FPY A 501
source : AC2

14) chain A
residue 313
type
sequence D
description BINDING SITE FOR RESIDUE FPY A 501
source : AC2

15) chain A
residue 319
type
sequence W
description BINDING SITE FOR RESIDUE FPY A 501
source : AC2

16) chain A
residue 128
type
sequence A
description BINDING SITE FOR RESIDUE GOL A 502
source : AC3

17) chain A
residue 134
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 502
source : AC3

18) chain A
residue 171
type
sequence E
description BINDING SITE FOR RESIDUE GOL A 502
source : AC3

19) chain A
residue 174
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 502
source : AC3

20) chain A
residue 175
type
sequence L
description BINDING SITE FOR RESIDUE GOL A 502
source : AC3

21) chain A
residue 60
type catalytic
sequence P
description 710
source MCSA : MCSA1

22) chain A
residue 62
type catalytic
sequence I
description 710
source MCSA : MCSA1

23) chain A
residue 155
type catalytic
sequence P
description 710
source MCSA : MCSA1

24) chain A
residue 213
type catalytic
sequence V
description 710
source MCSA : MCSA1

25) chain A
residue 216
type catalytic
sequence D
description 710
source MCSA : MCSA1

26) chain A
residue 312
type catalytic
sequence H
description 710
source MCSA : MCSA1

27) chain A
residue 216
type ACT_SITE
sequence D
description Proton donor => ECO:0000305|PubMed:11812140, ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715
source Swiss-Prot : SWS_FT_FI1

28) chain A
residue 245
type SITE
sequence S
description Activates the nucleophilic water => ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715
source Swiss-Prot : SWS_FT_FI5

29) chain A
residue 155
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:11812140, ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715
source Swiss-Prot : SWS_FT_FI3

30) chain A
residue 60
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14
source Swiss-Prot : SWS_FT_FI2

31) chain A
residue 62
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 213
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 312
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14
source Swiss-Prot : SWS_FT_FI2

34) chain A
residue 318
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:11812140, ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144
source Swiss-Prot : SWS_FT_FI4


Display surface

Download
Links