eF-site ID 1f0j-A
PDB Code 1f0j
Chain A

click to enlarge
Title CATALYTIC DOMAIN OF HUMAN PHOSPHODIESTERASE 4B2B
Classification HYDROLASE
Compound PHOSPHODIESTERASE 4B
Source Homo sapiens (Human) (PDE4B_HUMAN)
Sequence A:  SISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSHNRP
LTCIMYAIFQERDLLKTFRISSDTFITYMMTLEDHYHSDV
AYHNSLHAADVAQSTHVLLSTPALDAVFTDLEILAAIFAA
AIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVG
FKLLQEEHCDIFMNLTKKQRQTLRKMVIDMVLATDMSKHM
SLLADLKTMVETKKVTSSGVLLLDNYTDRIQVLRNMVHCA
DLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEISPM
CDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILD
TLEDNRNWYQSMIPQAPANRDCQGLMEKFQF
Description


Functional site

1) chain A
residue 238
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1101
source : AC1

2) chain A
residue 274
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1101
source : AC1

3) chain A
residue 275
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 1101
source : AC1

4) chain A
residue 392
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 1101
source : AC1

5) chain A
residue 275
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1102
source : AC2

6) chain A
residue 234
type
sequence H
description BINDING SITE FOR RESIDUE ARS A 1103
source : AC5

7) chain A
residue 392
type
sequence D
description BINDING SITE FOR RESIDUE ARS A 1103
source : AC5

8) chain A
residue 194
type
sequence C
description BINDING SITE FOR RESIDUE ARS A 1111
source : AC6

9) chain A
residue 499
type
sequence C
description BINDING SITE FOR RESIDUE ARS A 1212
source : AC9

10) 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

11) 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

12) 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

13) chain A
residue 275
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:15003452, ECO:0007744|PDB:1ROR
source Swiss-Prot : SWS_FT_FI5

14) 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

15) 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

16) chain A
residue 487
type MOD_RES
sequence A
description Phosphoserine => ECO:0000250|UniProtKB:P14646
source Swiss-Prot : SWS_FT_FI8

17) chain A
residue 489
type MOD_RES
sequence A
description Phosphoserine => ECO:0000250|UniProtKB:P14646
source Swiss-Prot : SWS_FT_FI8

18) chain A
residue 274-285
type prosite
sequence HDVDHPGVSNQF
description PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF
source prosite : PS00126

19) 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

20) 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


Display surface

Download
Links