eF-site ID 6njh-ABCD
PDB Code 6njh
Chain A, B, C, D

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Title Crystal Structure of the PDE4D Catalytic Domain and UCR2 Regulatory Helix with T-48
Classification HYDROLASE/HYDROLASE INHIBITOR
Compound cAMP-specific 3',5'-cyclic phosphodiesterase 4D
Source (PDE4D_HUMAN)
Sequence A:  QEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQ
ERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAAD
VVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGV
SNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCD
IFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMV
ETKKVTVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYR
QWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQV
GFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTI
PNQVSEFISNTFLD
B:  EQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIF
QERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAA
DVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPG
VSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENC
DIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTM
VETKKVTVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLY
RQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQ
VGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQST
IPNQVSEFISNTFLD
C:  QEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQ
ERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAAD
VVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGV
SNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCD
IFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMV
ETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQ
LYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEK
SQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQ
STIPNQVSEFISNTFLD
D:  EDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQE
RDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADV
VQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVS
NQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDI
FQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVE
TKKVTVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQ
WTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQVG
FIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIP
NQVSEFISNTFLD
Description


Functional site

1) chain A
residue 330
type
sequence H
description binding site for residue ZN A 701
source : AC1

2) chain A
residue 366
type
sequence H
description binding site for residue ZN A 701
source : AC1

3) chain A
residue 367
type
sequence D
description binding site for residue ZN A 701
source : AC1

4) chain A
residue 484
type
sequence D
description binding site for residue ZN A 701
source : AC1

5) chain A
residue 367
type
sequence D
description binding site for residue MG A 702
source : AC2

6) chain A
residue 326
type
sequence H
description binding site for residue KRD A 703
source : AC3

7) chain A
residue 487
type
sequence N
description binding site for residue KRD A 703
source : AC3

8) chain A
residue 499
type
sequence T
description binding site for residue KRD A 703
source : AC3

9) chain A
residue 506
type
sequence F
description binding site for residue KRD A 703
source : AC3

10) chain A
residue 535
type
sequence Q
description binding site for residue KRD A 703
source : AC3

11) chain A
residue 538
type
sequence F
description binding site for residue KRD A 703
source : AC3

12) chain A
residue 599
type
sequence F
description binding site for residue KRD A 703
source : AC3

13) chain A
residue 384
type
sequence E
description binding site for residue MG A 704
source : AC4

14) chain C
residue 318
type
sequence H
description binding site for residue MG A 704
source : AC4

15) chain B
residue 330
type
sequence H
description binding site for residue ZN B 701
source : AC5

16) chain B
residue 366
type
sequence H
description binding site for residue ZN B 701
source : AC5

17) chain B
residue 367
type
sequence D
description binding site for residue ZN B 701
source : AC5

18) chain B
residue 484
type
sequence D
description binding site for residue ZN B 701
source : AC5

19) chain B
residue 367
type
sequence D
description binding site for residue MG B 702
source : AC6

20) chain B
residue 326
type
sequence H
description binding site for residue KRD B 703
source : AC7

21) chain B
residue 487
type
sequence N
description binding site for residue KRD B 703
source : AC7

22) chain B
residue 498
type
sequence W
description binding site for residue KRD B 703
source : AC7

23) chain B
residue 499
type
sequence T
description binding site for residue KRD B 703
source : AC7

24) chain B
residue 502
type
sequence I
description binding site for residue KRD B 703
source : AC7

25) chain B
residue 506
type
sequence F
description binding site for residue KRD B 703
source : AC7

26) chain B
residue 523
type
sequence M
description binding site for residue KRD B 703
source : AC7

27) chain B
residue 535
type
sequence Q
description binding site for residue KRD B 703
source : AC7

28) chain B
residue 538
type
sequence F
description binding site for residue KRD B 703
source : AC7

29) chain B
residue 599
type
sequence F
description binding site for residue KRD B 703
source : AC7

30) chain B
residue 600
type
sequence I
description binding site for residue KRD B 703
source : AC7

31) chain C
residue 330
type
sequence H
description binding site for residue ZN C 700
source : AC8

32) chain C
residue 366
type
sequence H
description binding site for residue ZN C 700
source : AC8

33) chain C
residue 367
type
sequence D
description binding site for residue ZN C 700
source : AC8

34) chain C
residue 484
type
sequence D
description binding site for residue ZN C 700
source : AC8

35) chain C
residue 367
type
sequence D
description binding site for residue MG C 701
source : AC9

36) chain C
residue 326
type
sequence H
description binding site for residue KRD C 702
source : AD1

37) chain C
residue 487
type
sequence N
description binding site for residue KRD C 702
source : AD1

38) chain C
residue 499
type
sequence T
description binding site for residue KRD C 702
source : AD1

39) chain C
residue 502
type
sequence I
description binding site for residue KRD C 702
source : AD1

40) chain C
residue 506
type
sequence F
description binding site for residue KRD C 702
source : AD1

41) chain C
residue 523
type
sequence M
description binding site for residue KRD C 702
source : AD1

42) chain C
residue 535
type
sequence Q
description binding site for residue KRD C 702
source : AD1

43) chain C
residue 538
type
sequence F
description binding site for residue KRD C 702
source : AD1

44) chain C
residue 599
type
sequence F
description binding site for residue KRD C 702
source : AD1

45) chain B
residue 318
type
sequence H
description binding site for residue MG D 701
source : AD2

46) chain D
residue 384
type
sequence E
description binding site for residue MG D 701
source : AD2

47) chain D
residue 330
type
sequence H
description binding site for residue ZN D 702
source : AD3

48) chain D
residue 366
type
sequence H
description binding site for residue ZN D 702
source : AD3

49) chain D
residue 367
type
sequence D
description binding site for residue ZN D 702
source : AD3

50) chain D
residue 484
type
sequence D
description binding site for residue ZN D 702
source : AD3

51) chain D
residue 367
type
sequence D
description binding site for residue MG D 703
source : AD4

52) chain D
residue 326
type
sequence H
description binding site for residue KRD D 704
source : AD5

53) chain D
residue 374
type
sequence S
description binding site for residue KRD D 704
source : AD5

54) chain D
residue 487
type
sequence N
description binding site for residue KRD D 704
source : AD5

55) chain D
residue 498
type
sequence W
description binding site for residue KRD D 704
source : AD5

56) chain D
residue 499
type
sequence T
description binding site for residue KRD D 704
source : AD5

57) chain D
residue 523
type
sequence M
description binding site for residue KRD D 704
source : AD5

58) chain D
residue 535
type
sequence Q
description binding site for residue KRD D 704
source : AD5

59) chain D
residue 538
type
sequence F
description binding site for residue KRD D 704
source : AD5

60) chain D
residue 599
type
sequence F
description binding site for residue KRD D 704
source : AD5

61) chain A
residue 366-377
type prosite
sequence HDVDHPGVSNQF
description PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF
source prosite : PS00126

62) chain A
residue 387
type ACT_SITE
sequence L
description Proton donor => ECO:0000250|UniProtKB:Q07343
source Swiss-Prot : SWS_FT_FI1

63) chain B
residue 387
type ACT_SITE
sequence L
description Proton donor => ECO:0000250|UniProtKB:Q07343
source Swiss-Prot : SWS_FT_FI1

64) chain C
residue 387
type ACT_SITE
sequence L
description Proton donor => ECO:0000250|UniProtKB:Q07343
source Swiss-Prot : SWS_FT_FI1

65) chain D
residue 387
type ACT_SITE
sequence L
description Proton donor => ECO:0000250|UniProtKB:Q07343
source Swiss-Prot : SWS_FT_FI1

66) chain A
residue 387
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7
source Swiss-Prot : SWS_FT_FI2

67) chain A
residue 548
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7
source Swiss-Prot : SWS_FT_FI2

68) chain B
residue 387
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7
source Swiss-Prot : SWS_FT_FI2

69) chain B
residue 548
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7
source Swiss-Prot : SWS_FT_FI2

70) chain C
residue 387
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7
source Swiss-Prot : SWS_FT_FI2

71) chain C
residue 548
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7
source Swiss-Prot : SWS_FT_FI2

72) chain D
residue 387
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7
source Swiss-Prot : SWS_FT_FI2

73) chain D
residue 548
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7
source Swiss-Prot : SWS_FT_FI2

74) chain A
residue 391
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:2PW3
source Swiss-Prot : SWS_FT_FI3

75) chain B
residue 391
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:2PW3
source Swiss-Prot : SWS_FT_FI3

76) chain C
residue 391
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:2PW3
source Swiss-Prot : SWS_FT_FI3

77) chain D
residue 391
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:2PW3
source Swiss-Prot : SWS_FT_FI3

78) chain A
residue 427
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3
source Swiss-Prot : SWS_FT_FI4

79) chain A
residue 545
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3
source Swiss-Prot : SWS_FT_FI4

80) chain B
residue 427
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3
source Swiss-Prot : SWS_FT_FI4

81) chain B
residue 545
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3
source Swiss-Prot : SWS_FT_FI4

82) chain C
residue 427
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3
source Swiss-Prot : SWS_FT_FI4

83) chain C
residue 545
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3
source Swiss-Prot : SWS_FT_FI4

84) chain D
residue 427
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3
source Swiss-Prot : SWS_FT_FI4

85) chain D
residue 545
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3
source Swiss-Prot : SWS_FT_FI4

86) chain A
residue 428
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW
source Swiss-Prot : SWS_FT_FI5

87) chain B
residue 428
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW
source Swiss-Prot : SWS_FT_FI5

88) chain C
residue 428
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW
source Swiss-Prot : SWS_FT_FI5

89) chain D
residue 428
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW
source Swiss-Prot : SWS_FT_FI5

90) chain A
residue 273
type MOD_RES
sequence F
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

91) chain A
residue 300
type MOD_RES
sequence T
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

92) chain B
residue 273
type MOD_RES
sequence F
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

93) chain B
residue 300
type MOD_RES
sequence T
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

94) chain C
residue 273
type MOD_RES
sequence F
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

95) chain C
residue 300
type MOD_RES
sequence T
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

96) chain D
residue 273
type MOD_RES
sequence F
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

97) chain D
residue 300
type MOD_RES
sequence T
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

98) chain A
residue 312
type CROSSLNK
sequence L
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
source Swiss-Prot : SWS_FT_FI7

99) chain B
residue 312
type CROSSLNK
sequence L
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
source Swiss-Prot : SWS_FT_FI7

100) chain C
residue 312
type CROSSLNK
sequence L
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
source Swiss-Prot : SWS_FT_FI7

101) chain D
residue 312
type CROSSLNK
sequence L
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
source Swiss-Prot : SWS_FT_FI7


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