eF-site ID 3riy-ABCD
PDB Code 3riy
Chain A, B, C, D

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Title Sirt5 is an NAD-dependent protein lysine demalonylase and desuccinylase
Classification HYDROLASE
Compound NAD-dependent deacetylase sirtuin-5
Source Homo sapiens (Human) (3RIY)
Sequence A:  SFTARPSSSMADFRKFFAKAKHIVIISGAGVSAESGVPTF
RGAGGYWRKWQAQDLATPLAFAHNPSRVWEFYHYRREVMG
SKEPNAGHRAIAECETRLGKQGRRVVVITQNIDELHRKAG
TKNLLEIHGSLFKTRCTSCGVVAENYKSPICPALSGKGAP
EPGTQDASIPVEKLPRCEEAGCGGLLRPHVVWFGENLDPA
ILEEVDRELAHCDLCLVVGTSSVVYPAAMFAPQVAARGVP
VAEFNTETTPATNRFRFHFQGPCGTTLPEALA
B:  SFTARPSSSMADFRKFFAKAKHIVIISGAGVSAESGVPTF
RGAGGYWRKWQAQDLATPLAFAHNPSRVWEFYHYRREVMG
SKEPNAGHRAIAECETRLGKQGRRVVVITQNIDELHRKAG
TKNLLEIHGSLFKTRCTSCGVVAENYKSPICPALSGKGAP
EPGTQDASIPVEKLPRCEEAGCGGLLRPHVVWFGENLDPA
ILEEVDRELAHCDLCLVVGTSSVVYPAAMFAPQVAARGVP
VAEFNTETTPATNRFRFHFQGPCGTTLPEALA
C:  TARXSTG
D:  TARXSTGG
Description


Functional site

1) chain A
residue 166
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1001
source : AC1

2) chain A
residue 169
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1001
source : AC1

3) chain A
residue 207
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1001
source : AC1

4) chain A
residue 212
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1001
source : AC1

5) chain A
residue 59
type
sequence A
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

6) chain A
residue 60
type
sequence G
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

7) chain A
residue 64
type
sequence E
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

8) chain A
residue 67
type
sequence V
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

9) chain A
residue 68
type
sequence P
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

10) chain A
residue 69
type
sequence T
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

11) chain A
residue 70
type
sequence F
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

12) chain A
residue 71
type
sequence R
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

13) chain A
residue 140
type
sequence Q
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

14) chain A
residue 141
type
sequence N
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

15) chain A
residue 142
type
sequence I
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

16) chain A
residue 143
type
sequence D
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

17) chain A
residue 249
type
sequence G
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

18) chain A
residue 250
type
sequence T
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

19) chain A
residue 251
type
sequence S
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

20) chain A
residue 275
type
sequence N
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

21) chain A
residue 276
type
sequence T
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

22) chain A
residue 277
type
sequence E
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

23) chain A
residue 292
type
sequence P
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

24) chain A
residue 293
type
sequence C
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

25) chain D
residue 9
type
sequence X
description BINDING SITE FOR RESIDUE NAD A 2001
source : AC2

26) chain B
residue 166
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1002
source : AC3

27) chain B
residue 169
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1002
source : AC3

28) chain B
residue 207
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1002
source : AC3

29) chain B
residue 212
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1002
source : AC3

30) chain B
residue 59
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

31) chain B
residue 60
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

32) chain B
residue 64
type
sequence E
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

33) chain B
residue 67
type
sequence V
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

34) chain B
residue 68
type
sequence P
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

35) chain B
residue 69
type
sequence T
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

36) chain B
residue 70
type
sequence F
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

37) chain B
residue 71
type
sequence R
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

38) chain B
residue 140
type
sequence Q
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

39) chain B
residue 141
type
sequence N
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

40) chain B
residue 142
type
sequence I
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

41) chain B
residue 143
type
sequence D
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

42) chain B
residue 158
type
sequence H
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

43) chain B
residue 249
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

44) chain B
residue 250
type
sequence T
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

45) chain B
residue 251
type
sequence S
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

46) chain B
residue 275
type
sequence N
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

47) chain B
residue 276
type
sequence T
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

48) chain B
residue 277
type
sequence E
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

49) chain B
residue 292
type
sequence P
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

50) chain B
residue 293
type
sequence C
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

51) chain C
residue 9
type
sequence X
description BINDING SITE FOR RESIDUE NAD B 2002
source : AC4

52) chain C
residue 9
type MOD_RES
sequence X
description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
source Swiss-Prot : SWS_FT_FI5

53) chain D
residue 9
type MOD_RES
sequence X
description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
source Swiss-Prot : SWS_FT_FI5

54) chain C
residue 10
type MOD_RES
sequence S
description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588
source Swiss-Prot : SWS_FT_FI6

55) chain D
residue 10
type MOD_RES
sequence S
description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588
source Swiss-Prot : SWS_FT_FI6

56) chain B
residue 293
type MOD_RES
sequence C
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI2

57) chain A
residue 249
type MOD_RES
sequence G
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI2

58) chain A
residue 275
type MOD_RES
sequence N
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI2

59) chain A
residue 293
type MOD_RES
sequence C
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI2

60) chain B
residue 58
type MOD_RES
sequence G
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI2

61) chain B
residue 140
type MOD_RES
sequence Q
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI2

62) chain B
residue 249
type MOD_RES
sequence G
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI2

63) chain B
residue 275
type MOD_RES
sequence N
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI2

64) chain C
residue 6
type MOD_RES
sequence T
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI3

65) chain B
residue 169
type MOD_RES
sequence C
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI3

66) chain B
residue 207
type MOD_RES
sequence C
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI3

67) chain B
residue 212
type MOD_RES
sequence C
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI3

68) chain D
residue 6
type MOD_RES
sequence T
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI3

69) chain A
residue 166
type MOD_RES
sequence C
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI3

70) chain A
residue 169
type MOD_RES
sequence C
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI3

71) chain A
residue 207
type MOD_RES
sequence C
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI3

72) chain A
residue 212
type MOD_RES
sequence C
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI3

73) chain B
residue 102
type MOD_RES
sequence Y
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI3

74) chain B
residue 105
type MOD_RES
sequence R
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI3

75) chain B
residue 166
type MOD_RES
sequence C
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI3

76) chain C
residue 8
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
source Swiss-Prot : SWS_FT_FI4

77) chain D
residue 8
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
source Swiss-Prot : SWS_FT_FI4

78) chain C
residue 11
type MOD_RES
sequence T
description Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803
source Swiss-Prot : SWS_FT_FI7

79) chain D
residue 11
type MOD_RES
sequence T
description Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803
source Swiss-Prot : SWS_FT_FI7


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