1TX9: Gpd prior to capsid assembly

gpd prior to capsid assembly. Determined by X-ray diffraction at 3.31 Å resolution. Released 26 Apr 2005.

Method: X-ray diffraction
Resolution: 3.31 Å
Organism: Enterobacteria phage phiX174
Chains: 2
Atoms: 2,125
Mol. weight: 33.64 kDa
Released: 26 Apr 2005

Explore 1TX9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1TX9 contains 17 α-helices and 2 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: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	5-23	19
α-helix	31-38	8
α-helix	48-59	12
α-helix	61-65	5
β-strand	74	1	1
α-helix	75-85	11
α-helix	88-97	10
β-strand	102	1	1
α-helix	104-109	6
α-helix	117-129	13

Chain B: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	7-10	4
α-helix	15-21	7
α-helix	31-38	8
α-helix	45-47	3
α-helix	48-64	17
α-helix	73-74	2
α-helix	75-85	11
α-helix	91-99	9
α-helix	117-129	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Scaffolding protein D	A, B	protein	151	Enterobacteria phage phiX174	P69486

Sequence of entity 1 (A, B), FASTA

>1TX9_1 Scaffolding protein D (chains A, B)
SQVTEQSVRFQTALASIKLIQASAVLDLTEDDFDFLTSNKVWIATDRSRARRCVEACVYG
TLDFVGYPRFPAPVEFIAAVIAYYVHPVNIQTACLIMEGAEFTENIINGVERPVKAAELF
AFTLRVRAGNTDVLTDAEENVRQKLRAEGVM

Primary citation

Conformational switching by the scaffolding protein D directs the assembly of bacteriophage phiX174. Morais, M.C., Fisher, M., Kanamaru, S. et al. Mol Cell (2004) 15:991-997. DOI 10.1016/j.molcel.2004.08.023 · PubMed

Other PDB entries of the same protein (UniProt P69486), best resolution first:

1AL0 3.5 Å, Procapsid of bacteriophage PHIX174
1CD3 3.5 Å, Procapsid of bacteriophage PHIX174
1M0F 16.0 Å, Structural Studies of Bacteriophage alpha3 Assembly, Cryo-electron microscopy

Browse structure collections

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