2PNN: Ankyrin Repeat Domain of Trpv1

Crystal Structure of the Ankyrin Repeat Domain of Trpv1. Determined by X-ray diffraction at 2.7 Å resolution. Released 3 Jul 2007.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Rattus norvegicus
Chains: 1
Atoms: 2,034
Mol. weight: 30.95 kDa
Ligands: ATP
Released: 3 Jul 2007

Explore 2PNN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2PNN contains 16 α-helices and 4 β-strands across 1 chain. 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: 16 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	114-122	9
α-helix	132-138	7
α-helix	146-148	3
α-helix	157-163	7
β-strand	166	1	1
β-strand	169	1	1
α-helix	171-182	12
α-helix	186-190	5
α-helix	204-210	7
α-helix	214-222	9
β-strand	231	1	2
α-helix	234-236	3
β-strand	249	1	2
α-helix	251-257	7
α-helix	261-269	9
α-helix	287-294	8
α-helix	299-319	21
α-helix	325-327	3
α-helix	336-342	7
α-helix	346-356	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transient receptor potential cation channel subfamily V member 1	A	protein	273	Rattus norvegicus	O35433 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2PNN_1 Transient receptor potential cation channel subfamily V member 1 (chains A)
SVSAGEKPPRLYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKDPETGKTCLLK
AMLNLHNGQNDTIALLLDVARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMTLVTLL
VENGADVQAAANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISAR
DSVGNTVLHALVEVADNTVDNTKFVTSMYNEILILGAKLHPTLKLEEITNRKGLTPLALA
ASSGKIGVLAYILQREIHEPECRHAAAHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1

Primary citation

The Ankyrin Repeats of TRPV1 Bind Multiple Ligands and Modulate Channel Sensitivity. Lishko, P.V., Procko, E., Jin, X. et al. Neuron (2007) 54:905-918. DOI 10.1016/j.neuron.2007.05.027 · PubMed

Other PDB entries of the same protein (UniProt O35433 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3SUI 1.95 Å, Crystal structure of ca2+-calmodulin in complex with a trpv1 c-terminal peptide
8U4D 2.2 Å, TRPV1 in nanodisc bound with PI-Br4, consensus structure
8U3A 2.3 Å, TRPV1 in nanodisc bound with PI-Br4 bound in Conformation 1 (monomer)
8U3C 2.3 Å, TRPV1 in nanodisc bound with PI-Br4 bound in Conformation 2 (monomer)
8U43 2.4 Å, TRPV1 in nanodisc bound with PIP2-Br4
7L2P 2.6 Å, cryo-EM structure of unliganded minimal TRPV1
7L2H 2.63 Å, Cryo-EM structure of unliganded full-length TRPV1 at neutral pH
7LP9 2.63 Å, Cryo-EM structure of full-length TRPV1 at 4 degrees Celsius
9W4M 2.7 Å, ratTRPV1 bound with antagonist AMG517
7L2S 2.71 Å, cryo-EM structure of DkTx-bound minimal TRPV1 at the pre-bound state
7MZ5 2.76 Å, Cryo-EM structure of RTX-bound full-length TRPV1 in C2 state
9W4T 2.87 Å, ratTRPV1 bound with antagonist AMG9810

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