eF-site ID 6f8x-A
PDB Code 6f8x
Chain A

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Title Crystal structure of the PDE4D catalytic domain in complex with GEBR-26g
Classification HYDROLASE
Compound cAMP-specific 3',5'-cyclic phosphodiesterase 4D
Source Homo sapiens (Human) (PDE4D_HUMAN)
Sequence A:  DVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQER
DLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVV
QSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSN
QFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIF
QNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVET
KKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLY
RQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQ
VGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQST
IP
Description


Functional site

1) chain A
residue 330
type
sequence H
description binding site for residue ZN A 601
source : AC1

2) chain A
residue 366
type
sequence H
description binding site for residue ZN A 601
source : AC1

3) chain A
residue 367
type
sequence D
description binding site for residue ZN A 601
source : AC1

4) chain A
residue 484
type
sequence D
description binding site for residue ZN A 601
source : AC1

5) chain A
residue 367
type
sequence D
description binding site for residue MG A 602
source : AC2

6) chain A
residue 417
type
sequence N
description binding site for residue MG A 603
source : AC3

7) chain A
residue 467
type
sequence D
description binding site for residue MG A 604
source : AC4

8) chain A
residue 471
type
sequence D
description binding site for residue MG A 604
source : AC4

9) chain A
residue 527
type
sequence H
description binding site for residue MG A 604
source : AC4

10) chain A
residue 325
type
sequence Y
description binding site for residue D08 A 605
source : AC5

11) chain A
residue 326
type
sequence H
description binding site for residue D08 A 605
source : AC5

12) chain A
residue 374
type
sequence S
description binding site for residue D08 A 605
source : AC5

13) chain A
residue 375
type
sequence N
description binding site for residue D08 A 605
source : AC5

14) chain A
residue 439
type
sequence M
description binding site for residue D08 A 605
source : AC5

15) chain A
residue 487
type
sequence N
description binding site for residue D08 A 605
source : AC5

16) chain A
residue 502
type
sequence I
description binding site for residue D08 A 605
source : AC5

17) chain A
residue 503
type
sequence M
description binding site for residue D08 A 605
source : AC5

18) chain A
residue 506
type
sequence F
description binding site for residue D08 A 605
source : AC5

19) chain A
residue 523
type
sequence M
description binding site for residue D08 A 605
source : AC5

20) chain A
residue 534
type
sequence S
description binding site for residue D08 A 605
source : AC5

21) chain A
residue 535
type
sequence Q
description binding site for residue D08 A 605
source : AC5

22) chain A
residue 538
type
sequence F
description binding site for residue D08 A 605
source : AC5

23) chain A
residue 509
type
sequence Q
description binding site for residue EDO A 606
source : AC6

24) chain A
residue 522
type
sequence P
description binding site for residue EDO A 606
source : AC6

25) chain A
residue 524
type
sequence C
description binding site for residue EDO A 606
source : AC6

26) chain A
residue 461
type
sequence S
description binding site for residue EDO A 607
source : AC7

27) chain A
residue 462
type
sequence G
description binding site for residue EDO A 607
source : AC7

28) chain A
residue 554
type
sequence V
description binding site for residue EDO A 607
source : AC7

29) chain A
residue 555
type
sequence H
description binding site for residue EDO A 607
source : AC7

30) chain A
residue 557
type
sequence D
description binding site for residue EDO A 607
source : AC7

31) chain A
residue 567
type
sequence D
description binding site for residue DMS B 603
source : AD1

32) chain A
residue 462
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 466
type BINDING
sequence L
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

34) chain A
residue 462
type ACT_SITE
sequence G
description Proton donor => ECO:0000250|UniProtKB:Q07343
source Swiss-Prot : SWS_FT_FI1

35) chain A
residue 299
type MOD_RES
sequence K
description Phosphoserine => ECO:0007744|PubMed:21406692
source Swiss-Prot : SWS_FT_FI6

36) chain A
residue 301
type MOD_RES
sequence F
description Phosphoserine => ECO:0007744|PubMed:21406692
source Swiss-Prot : SWS_FT_FI6

37) chain A
residue 348
type MOD_RES
sequence E
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI7

38) chain A
residue 375
type MOD_RES
sequence N
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI7

39) chain A
residue 387
type CROSSLNK
sequence L
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
source Swiss-Prot : SWS_FT_FI8

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

41) chain A
residue 502
type BINDING
sequence I
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

42) chain A
residue 503
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW
source Swiss-Prot : SWS_FT_FI5


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