3PHU: RNA-directed RNA polymerase L

OTU Domain of Crimean Congo Hemorrhagic Fever Virus. Determined by X-ray diffraction at 2.2 Å resolution. Released 2 Feb 2011.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Crimean-Congo hemorrhagic fever virus strain IbAr10200
Chains: 2
Atoms: 3,091
Mol. weight: 49.61 kDa
Released: 2 Feb 2011

Explore 3PHU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3PHU contains 21 α-helices and 18 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: 10 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	1-5	5
β-strand	10-13	4	1
β-strand	16-19	4	1
β-strand	24	1	2
α-helix	25-28	4
β-strand	29-32	4	1
α-helix	40-49	10
α-helix	58-72	15
α-helix	73-75	3
α-helix	77-82	6
α-helix	86-94	9
α-helix	98-100	3
α-helix	102-111	10
β-strand	116-121	6	1
β-strand	126	1	2
β-strand	127-133	7	1
β-strand	142-147	6	1
β-strand	151-157	7	1
α-helix	171-182	12

Chain B: 11 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
β-strand	10-13	4	3
β-strand	16-19	4	3
β-strand	24	1	4
α-helix	25-28	4
β-strand	29-32	4	3
α-helix	40-47	8
α-helix	58-72	15
α-helix	73-75	3
α-helix	77-82	6
α-helix	86-94	9
α-helix	98-100	3
α-helix	102-111	10
β-strand	116-120	5	3
β-strand	126	1	4
β-strand	129-133	5	3
β-strand	142-147	6	3
β-strand	151-157	7	3
α-helix	158	1
α-helix	171-181	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RNA-directed RNA polymerase L	A, B	protein	219	Crimean-Congo hemorrhagic fever virus strain IbAr10200	Q6TQR6 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3PHU_1 RNA-directed RNA polymerase L (chains A, B)
GPMDFLRSLDWTQVIAGQYVSNPRFNISDYFEIVRQPGDGNCFYHSIAELTMPNKTDHSY
HYIKRLTESAARKYYQEEPEARLVGLSLEDYLKRMLSDNEWGSTLEASMLAKEMGITIII
WTVAASDEVEAGIKFGDGDVFTAVNLLHSGQTHFDALRILPQFETDTREALSLMDRVIAV
DQLTSSSSDELQDYEDLALALTSAEESNRRSSLDEVTLS

Primary citation

Molecular basis for ubiquitin and ISG15 cross-reactivity in viral ovarian tumor domains. Akutsu, M., Ye, Y., Virdee, S. et al. Proc Natl Acad Sci U S A (2011) 108:2228-2233. DOI 10.1073/pnas.1015287108 · PubMed

Other PDB entries of the same protein (UniProt Q6TQR6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5V5H 1.5 Å, OTU protease of Crimean Congo Hemorrhagic Fever Virus bound to ubiquitin variant CC.2
3PHX 1.6 Å, OTU Domain of Crimean Congo Hemorrhagic Fever Virus in complex with ISG15
3PRP 1.7 Å, Structural analysis of a viral OTU domain protease from the Crimean-Congo Hemorrhagic…
3PHW 2.0 Å, OTU Domain of Crimean Congo Hemorrhagic Fever Virus in complex with Ubiquitin
5V5G 2.1 Å, OTU protease of Crimean Congo Hemorrhagic Fever Virus bound to ubiquitin variant CC.4
5V5I 2.2 Å, OTU protease of Crimean Congo Hemorrhagic Fever Virus bound to ubiquitin variant CC.1
3PRM 2.3 Å, Structural analysis of a viral OTU domain protease from the Crimean-Congo Hemorrhagic…
3PSE 2.3 Å, Structure of a viral OTU domain protease bound to interferon-stimulated gene 15 (ISG15)
3ZNH 2.3 Å, Crimean Congo Hemorrhagic Fever Virus OTU domain in complex with ubiquitin-propargyl.
9T0E 2.3 Å, Structure of Crimean Congo hemorrhagic fever virus (CCHFV) L protein bound to 5' vRNA…
22TH 2.5 Å, Cryo-EM structure of Crimean-Congo hemorrhagic fever virus RNA polymerase in complex…
3PT2 2.5 Å, Structure of a viral OTU domain protease bound to Ubiquitin

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