eF-site ID 1p6o-B
PDB Code 1p6o
Chain B

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Title The crystal structure of yeast cytosine deaminase bound to 4(R)-hydroxyl-3,4-dihydropyrimidine at 1.14 angstroms.
Classification HYDROLASE
Compound Cytosine deaminase
Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (FCY1_YEAST)
Sequence B:  GSSMVTGGMASKWDQKGMDIAYEEAALGYKEGGVPIGGCL
INNKDGSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGK
VYKDTTLYTTLSPCDMCTGAIIMYGIPRCVVGENVNFKSK
GEKYLQTRGHEVVVVDDERCKKIMKQFIDERPQDWFEDIG
E
Description


Functional site

1) chain B
residue 262
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 400
source : AC1

2) chain B
residue 291
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 400
source : AC1

3) chain B
residue 294
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 400
source : AC1

4) chain B
residue 328
type
sequence E
description BINDING SITE FOR RESIDUE CA B 402
source : AC3

5) chain B
residue 350
type
sequence Q
description BINDING SITE FOR RESIDUE CA B 402
source : AC3

6) chain B
residue 275
type
sequence E
description BINDING SITE FOR RESIDUE CA B 403
source : AC4

7) chain B
residue 233
type
sequence I
description BINDING SITE FOR RESIDUE HPY B 410
source : AC5

8) chain B
residue 251
type
sequence N
description BINDING SITE FOR RESIDUE HPY B 410
source : AC5

9) chain B
residue 262
type
sequence H
description BINDING SITE FOR RESIDUE HPY B 410
source : AC5

10) chain B
residue 263
type
sequence G
description BINDING SITE FOR RESIDUE HPY B 410
source : AC5

11) chain B
residue 264
type
sequence E
description BINDING SITE FOR RESIDUE HPY B 410
source : AC5

12) chain B
residue 290
type
sequence P
description BINDING SITE FOR RESIDUE HPY B 410
source : AC5

13) chain B
residue 291
type
sequence C
description BINDING SITE FOR RESIDUE HPY B 410
source : AC5

14) chain B
residue 294
type
sequence C
description BINDING SITE FOR RESIDUE HPY B 410
source : AC5

15) chain B
residue 355
type
sequence D
description BINDING SITE FOR RESIDUE HPY B 410
source : AC5

16) chain B
residue 273
type
sequence R
description BINDING SITE FOR RESIDUE ACY A 420
source : AC7

17) chain B
residue 302
type
sequence G
description BINDING SITE FOR RESIDUE ACY B 421
source : AC8

18) chain B
residue 326
type
sequence G
description BINDING SITE FOR RESIDUE ACY B 421
source : AC8

19) chain B
residue 327
type
sequence H
description BINDING SITE FOR RESIDUE ACY B 421
source : AC8

20) chain B
residue 353
type
sequence F
description BINDING SITE FOR RESIDUE ACY B 421
source : AC8

21) chain B
residue 240
type
sequence N
description BINDING SITE FOR RESIDUE ACY B 422
source : AC9

22) chain B
residue 281
type
sequence D
description BINDING SITE FOR RESIDUE ACY B 422
source : AC9

23) chain B
residue 304
type
sequence P
description BINDING SITE FOR RESIDUE ACY B 422
source : AC9

24) chain B
residue 353
type
sequence F
description BINDING SITE FOR RESIDUE ACY B 422
source : AC9

25) chain B
residue 262
type catalytic
sequence H
description 636
source MCSA : MCSA2

26) chain B
residue 264
type catalytic
sequence E
description 636
source MCSA : MCSA2

27) chain B
residue 289
type catalytic
sequence S
description 636
source MCSA : MCSA2

28) chain B
residue 291
type catalytic
sequence C
description 636
source MCSA : MCSA2

29) chain B
residue 294
type catalytic
sequence C
description 636
source MCSA : MCSA2

30) chain B
residue 264
type ACT_SITE
sequence E
description Proton donor => ECO:0000269|PubMed:12637534, ECO:0007744|PDB:1UAQ
source Swiss-Prot : SWS_FT_FI1

31) chain B
residue 262
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0000269|PubMed:15879217, ECO:0007744|PDB:1OX7, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1RB7, ECO:0007744|PDB:1UAQ, ECO:0007744|PDB:1YSB, ECO:0007744|PDB:1YSD
source Swiss-Prot : SWS_FT_FI3

32) chain B
residue 291
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0000269|PubMed:15879217, ECO:0007744|PDB:1OX7, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1RB7, ECO:0007744|PDB:1UAQ, ECO:0007744|PDB:1YSB, ECO:0007744|PDB:1YSD
source Swiss-Prot : SWS_FT_FI3

33) chain B
residue 294
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0000269|PubMed:15879217, ECO:0007744|PDB:1OX7, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1RB7, ECO:0007744|PDB:1UAQ, ECO:0007744|PDB:1YSB, ECO:0007744|PDB:1YSD
source Swiss-Prot : SWS_FT_FI3

34) chain B
residue 251
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1UAQ
source Swiss-Prot : SWS_FT_FI2

35) chain B
residue 355
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1UAQ
source Swiss-Prot : SWS_FT_FI2


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