eF-site ID 6f8u-B
PDB Code 6f8u
Chain B

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Title Crystal structure of the PDE4D catalytic domain in complex with GEBR-20b
Classification HYDROLASE
Compound cAMP-specific 3',5'-cyclic phosphodiesterase 4D
Source Homo sapiens (Human) (PDE4D_HUMAN)
Sequence B:  DVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQER
DLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVV
QSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSN
QFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIF
QNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVET
KKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLY
RQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQ
VGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQST
IPQAH
Description


Functional site

1) chain B
residue 330
type
sequence H
description binding site for residue ZN B 601
source : AC7

2) chain B
residue 366
type
sequence H
description binding site for residue ZN B 601
source : AC7

3) chain B
residue 367
type
sequence D
description binding site for residue ZN B 601
source : AC7

4) chain B
residue 484
type
sequence D
description binding site for residue ZN B 601
source : AC7

5) chain B
residue 367
type
sequence D
description binding site for residue MG B 602
source : AC8

6) chain B
residue 325
type
sequence Y
description binding site for residue CZQ B 603
source : AC9

7) chain B
residue 439
type
sequence M
description binding site for residue CZQ B 603
source : AC9

8) chain B
residue 487
type
sequence N
description binding site for residue CZQ B 603
source : AC9

9) chain B
residue 495
type
sequence Y
description binding site for residue CZQ B 603
source : AC9

10) chain B
residue 498
type
sequence W
description binding site for residue CZQ B 603
source : AC9

11) chain B
residue 499
type
sequence T
description binding site for residue CZQ B 603
source : AC9

12) chain B
residue 502
type
sequence I
description binding site for residue CZQ B 603
source : AC9

13) chain B
residue 503
type
sequence M
description binding site for residue CZQ B 603
source : AC9

14) chain B
residue 506
type
sequence F
description binding site for residue CZQ B 603
source : AC9

15) chain B
residue 523
type
sequence M
description binding site for residue CZQ B 603
source : AC9

16) chain B
residue 535
type
sequence Q
description binding site for residue CZQ B 603
source : AC9

17) chain B
residue 538
type
sequence F
description binding site for residue CZQ B 603
source : AC9

18) chain B
residue 542
type
sequence I
description binding site for residue CZQ B 603
source : AC9

19) chain B
residue 325
type
sequence Y
description binding site for residue CZQ B 604
source : AD1

20) chain B
residue 374
type
sequence S
description binding site for residue CZQ B 604
source : AD1

21) chain B
residue 487
type
sequence N
description binding site for residue CZQ B 604
source : AD1

22) chain B
residue 488
type
sequence P
description binding site for residue CZQ B 604
source : AD1

23) chain B
residue 495
type
sequence Y
description binding site for residue CZQ B 604
source : AD1

24) chain B
residue 498
type
sequence W
description binding site for residue CZQ B 604
source : AD1

25) chain B
residue 499
type
sequence T
description binding site for residue CZQ B 604
source : AD1

26) chain B
residue 502
type
sequence I
description binding site for residue CZQ B 604
source : AD1

27) chain B
residue 503
type
sequence M
description binding site for residue CZQ B 604
source : AD1

28) chain B
residue 506
type
sequence F
description binding site for residue CZQ B 604
source : AD1

29) chain B
residue 522
type
sequence P
description binding site for residue CZQ B 604
source : AD1

30) chain B
residue 523
type
sequence M
description binding site for residue CZQ B 604
source : AD1

31) chain B
residue 534
type
sequence S
description binding site for residue CZQ B 604
source : AD1

32) chain B
residue 535
type
sequence Q
description binding site for residue CZQ B 604
source : AD1

33) chain B
residue 538
type
sequence F
description binding site for residue CZQ B 604
source : AD1

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

35) chain B
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

36) chain B
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

37) chain B
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

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

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

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

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

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

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


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