1XLZ: Catalytic Domain Of Human Phosphodiesterase 4B

Catalytic Domain Of Human Phosphodiesterase 4B In Complex With Filaminast. Determined by X-ray diffraction at 2.06 Å resolution. Released 14 Dec 2004.

Method
X-ray diffraction
Resolution
2.06 Å
Organism
Homo sapiens
Chains
2
Atoms
5,424
Mol. weight
92.38 kDa
Ligands
FIL, MG, ZN
Released
14 Dec 2004

Explore 1XLZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1XLZ contains 48 α-helices and 4 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 24 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix164-1707
α-helix180-1856
α-helix191-20212
α-helix205-2084
α-helix213-22513
α-helix236-24914
α-helix253-2553
α-helix261-27313
α-helix283-2886
α-helix292-2965
α-helix302-31413
α-helix318-3203
α-helix328-34316
α-helix347-3493
α-helix350-36213
β-strand36611
β-strand37211
α-helix377-39216
α-helix395-3973
α-helix400-42324
α-helix426-4294
α-helix430-4323
α-helix439-4468
α-helix447-4515
α-helix452-46110
α-helix467-48216
Chain B: 24 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix164-1707
α-helix180-1867
α-helix191-20212
α-helix205-2084
α-helix213-22513
α-helix236-24914
α-helix253-2553
α-helix261-27313
α-helix283-2886
α-helix292-2976
α-helix302-31312
α-helix318-3203
α-helix328-34316
α-helix347-3493
α-helix350-36213
β-strand36612
β-strand37212
α-helix377-39216
α-helix395-3973
α-helix400-42324
α-helix426-4294
α-helix430-4323
α-helix439-4468
α-helix447-4515
α-helix452-46211
α-helix467-48216

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
cAMP-specific 3',5'-cyclic phosphodiesterase 4BA, Bprotein398Homo sapiensQ07343 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1XLZ_1 cAMP-specific 3',5'-cyclic phosphodiesterase 4B (chains A, B)
MGSSHHHHHHSSGLVPRGSHMSISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSHNR
PLTCIMYAIFQERDLLKTFRISSDTFITYMMTLEDHYHSDVAYHNSLHAADVAQSTHVLL
STPALDAVFTDLEILAAIFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAV
GFKLLQEEHCDIFMNLTKKQRQTLRKMVIDMVLATDMSKHMSLLADLKTMVETKKVTSSG
VLLLDNYTDRIQVLRNMVHCADLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEISP
MCDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILDTLEDNRNWYQSMIPQSPSP
PLDEQNRDCQGLMEKFQFELTLDEEDSEGPEKEGEGHS

Ligands and cofactors

IDNameFormulaCopies
FIL(1E)-1-[3-(cyclopentyloxy)-4-methoxyphenyl]ethanone O-(aminocarbonyl)oximeC15 H20 N2 O42
MGMagnesium ionMg2
ZNZinc ionZn2

Primary citation

Structural Basis for the Activity of Drugs that Inhibit Phosphodiesterases. Card, G.L., England, B.P., Suzuki, Y. et al. Structure (2004) 12:2233-2247. DOI 10.1016/j.str.2004.10.004 · PubMed

Other PDB entries of the same protein (UniProt Q07343 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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