eF-site ID 1ro9-AB
PDB Code 1ro9
Chain A, B

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Title CRYSTAL STRUCTURES OF THE CATALYTIC DOMAIN OF PHOSPHODIESTERASE 4B2B COMPLEXED WITH 8-Br-AMP
Classification HYDROLASE
Compound cAMP-specific 3',5'-cyclic phosphodiesterase 4B
Source Homo sapiens (Human) (PDE4B_HUMAN)
Sequence A:  SISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSHNRP
LTCIMYAIFQERDLLKTFRISSDTFITYMMTLEDHYHSDV
AYHNSLHAADVAQSTHVLLSTPALDAVFTDLEILAAIFAA
AIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVG
FKLLQEEHCDIFMNLTKKQRQTLRKMVIDMVLATDMSKHM
SLLADLKTMVETKKVTSSGVLLLDNYTDRIQVLRNMVHCA
DLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEISPM
CDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILD
TLEDNRNWYQSMIPQAPA
B:  SISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSHNRP
LTCIMYAIFQERDLLKTFRISSDTFITYMMTLEDHYHSDV
AYHNSLHAADVAQSTHVLLSTPALDAVFTDLEILAAIFAA
AIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVG
FKLLQEEHCDIFMNLTKKQRQTLRKMVIDMVLATDMSKHM
SLLADLKTMVETKKVTSSGVLLLDNYTDRIQVLRNMVHCA
DLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEISPM
CDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILD
TLEDNRNWYQSMIPQAP
Description


Functional site
1) chain A
residue 238
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 529
source : AC1
2) chain A
residue 274
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 529
source : AC1
3) chain A
residue 275
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 529
source : AC1
4) chain A
residue 392
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 529
source : AC1
5) chain A
residue 275
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 530
source : AC2
6) chain B
residue 238
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 529
source : AC3
7) chain B
residue 274
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 529
source : AC3
8) chain B
residue 275
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 529
source : AC3
9) chain B
residue 392
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 529
source : AC3
10) chain B
residue 275
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 530
source : AC4
11) chain A
residue 233
type
sequence Y
description BINDING SITE FOR RESIDUE 8BR A 531
source : AC5
12) chain A
residue 234
type
sequence H
description BINDING SITE FOR RESIDUE 8BR A 531
source : AC5
13) chain A
residue 392
type
sequence D
description BINDING SITE FOR RESIDUE 8BR A 531
source : AC5
14) chain A
residue 393
type
sequence L
description BINDING SITE FOR RESIDUE 8BR A 531
source : AC5
15) chain A
residue 395
type
sequence N
description BINDING SITE FOR RESIDUE 8BR A 531
source : AC5
16) chain A
residue 403
type
sequence Y
description BINDING SITE FOR RESIDUE 8BR A 531
source : AC5
17) chain A
residue 414
type
sequence F
description BINDING SITE FOR RESIDUE 8BR A 531
source : AC5
18) chain A
residue 443
type
sequence Q
description BINDING SITE FOR RESIDUE 8BR A 531
source : AC5
19) chain A
residue 446
type
sequence F
description BINDING SITE FOR RESIDUE 8BR A 531
source : AC5
20) chain B
residue 233
type
sequence Y
description BINDING SITE FOR RESIDUE 8BR B 531
source : AC6
21) chain B
residue 234
type
sequence H
description BINDING SITE FOR RESIDUE 8BR B 531
source : AC6
22) chain B
residue 238
type
sequence H
description BINDING SITE FOR RESIDUE 8BR B 531
source : AC6
23) chain B
residue 347
type
sequence M
description BINDING SITE FOR RESIDUE 8BR B 531
source : AC6
24) chain B
residue 392
type
sequence D
description BINDING SITE FOR RESIDUE 8BR B 531
source : AC6
25) chain B
residue 395
type
sequence N
description BINDING SITE FOR RESIDUE 8BR B 531
source : AC6
26) chain B
residue 403
type
sequence Y
description BINDING SITE FOR RESIDUE 8BR B 531
source : AC6
27) chain B
residue 410
type
sequence I
description BINDING SITE FOR RESIDUE 8BR B 531
source : AC6
28) chain B
residue 414
type
sequence F
description BINDING SITE FOR RESIDUE 8BR B 531
source : AC6
29) chain B
residue 443
type
sequence Q
description BINDING SITE FOR RESIDUE 8BR B 531
source : AC6
30) chain B
residue 446
type
sequence F
description BINDING SITE FOR RESIDUE 8BR B 531
source : AC6
31) chain A
residue 274-285
type prosite
sequence HDVDHPGVSNQF
description PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF
source prosite : PS00126
32) chain A
residue 234
type ACT_SITE
sequence H
description Proton donor => ECO:0000305|PubMed:15003452, ECO:0007744|PDB:1ROR
source Swiss-Prot : SWS_FT_FI1
33) chain B
residue 234
type ACT_SITE
sequence H
description Proton donor => ECO:0000305|PubMed:15003452, ECO:0007744|PDB:1ROR
source Swiss-Prot : SWS_FT_FI1
34) chain A
residue 234
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5
source Swiss-Prot : SWS_FT_FI2
35) chain A
residue 443
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5
source Swiss-Prot : SWS_FT_FI2
36) chain B
residue 234
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5
source Swiss-Prot : SWS_FT_FI2
37) chain B
residue 443
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5
source Swiss-Prot : SWS_FT_FI2
38) chain A
residue 238
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:17727341, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:2QYL, ECO:0007744|PDB:3D3P
source Swiss-Prot : SWS_FT_FI3
39) chain B
residue 238
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:17727341, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:2QYL, ECO:0007744|PDB:3D3P
source Swiss-Prot : SWS_FT_FI3
40) chain A
residue 274
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10846163, ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:17727341, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1F0J, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:2QYL, ECO:0007744|PDB:3D3P
source Swiss-Prot : SWS_FT_FI4
41) chain B
residue 274
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10846163, ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:17727341, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1F0J, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:2QYL, ECO:0007744|PDB:3D3P
source Swiss-Prot : SWS_FT_FI4
42) chain A
residue 275
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:15003452, ECO:0007744|PDB:1ROR
source Swiss-Prot : SWS_FT_FI5
43) chain B
residue 275
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:15003452, ECO:0007744|PDB:1ROR
source Swiss-Prot : SWS_FT_FI5
44) chain A
residue 392
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10846163, ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1F0J, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:3D3P
source Swiss-Prot : SWS_FT_FI6
45) chain B
residue 392
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10846163, ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1F0J, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:3D3P
source Swiss-Prot : SWS_FT_FI6
46) chain A
residue 446
type BINDING
sequence F
description BINDING => ECO:0000305|PubMed:15003452, ECO:0000305|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5
source Swiss-Prot : SWS_FT_FI7
47) chain B
residue 446
type BINDING
sequence F
description BINDING => ECO:0000305|PubMed:15003452, ECO:0000305|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5
source Swiss-Prot : SWS_FT_FI7
48) chain A
residue 487
type MOD_RES
sequence A
description Phosphoserine => ECO:0000250|UniProtKB:P14646
source Swiss-Prot : SWS_FT_FI8
49) chain A
residue 489
type MOD_RES
sequence A
description Phosphoserine => ECO:0000250|UniProtKB:P14646
source Swiss-Prot : SWS_FT_FI8
50) chain B
residue 487
type MOD_RES
sequence A
description Phosphoserine => ECO:0000250|UniProtKB:P14646
source Swiss-Prot : SWS_FT_FI8

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