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

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Title Crystal Structure of the PDE4D Catalytic Domain and UCR2 Regulatory Helix with T-49
Classification HYDROLASE/HYDROLASE INHIBITOR
Compound cAMP-specific 3',5'-cyclic phosphodiesterase 4D
Source (PDE4D_HUMAN)
Sequence A:  EQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIF
QERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAA
DVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPG
VSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENC
DIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTM
VETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPL
QLYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVE
KSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWY
QSTIPQNQVSEFISNTFLD
Description


Functional site

1) chain A
residue 330
type
sequence H
description binding site for residue ZN A 700
source : AC1

2) chain A
residue 366
type
sequence H
description binding site for residue ZN A 700
source : AC1

3) chain A
residue 367
type
sequence D
description binding site for residue ZN A 700
source : AC1

4) chain A
residue 484
type
sequence D
description binding site for residue ZN A 700
source : AC1

5) chain A
residue 367
type
sequence D
description binding site for residue MG A 701
source : AC2

6) chain A
residue 487
type
sequence N
description binding site for residue KR4 A 702
source : AC3

7) chain A
residue 499
type
sequence T
description binding site for residue KR4 A 702
source : AC3

8) chain A
residue 535
type
sequence Q
description binding site for residue KR4 A 702
source : AC3

9) chain A
residue 538
type
sequence F
description binding site for residue KR4 A 702
source : AC3

10) chain A
residue 599
type
sequence F
description binding site for residue KR4 A 702
source : AC3

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

12) 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

13) 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

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

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

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

17) 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

18) 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

19) 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

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

21) 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


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