4EQF: PEX5-related protein

Trip8b-1a#206-567 interacting with the carboxy-terminal seven residues of HCN2. Determined by X-ray diffraction at 3.0 Å resolution. Released 30 May 2012.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Mus musculus
Chains: 2
Atoms: 2,260
Mol. weight: 41.75 kDa
Released: 30 May 2012

Explore 4EQF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4EQF contains 18 α-helices and 0 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: 18 helices, 0 β-strands

Element	Residues	Length
α-helix	10-11	2
α-helix	22-32	11
α-helix	35-48	14
α-helix	53-65	13
α-helix	69-82	14
α-helix	87-99	13
α-helix	103-116	14
α-helix	118-121	4
α-helix	145-160	16
α-helix	167-180	14
α-helix	183-196	14
α-helix	201-213	13
α-helix	217-230	14
α-helix	235-248	14
α-helix	252-266	15
α-helix	282-294	13
α-helix	297-304	8
α-helix	309-311	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
PEX5-related protein	A	protein	365	Mus musculus	Q8C437 (AlphaFold model)
Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2	B	protein	7	Mus musculus	O88703 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4EQF_1 PEX5-related protein (chains A)
GAMEFERAKAAVESDTEFWDKMQAEWEEMARRNWISENQEAQNQVTVSASEKGYYFHTEN
PFKDWPGAFEEGLKRLKEGDLPVTILFMEAAILQDPGDAEAWQFLGITQAENENEQAAIV
ALQRCLELQPNNLKALMALAVSYTNTSHQQDACEALKNWIKQNPKYKYLVKNKKGSPGLT
RRMSKSPVDSSVLEGVKELYLEAAHQNGDMIDPDLQTGLGVLFHLSGEFNRAIDAFNAAL
TVRPEDYSLWNRLGATLANGDRSEEAVEAYTRALEIQPGFIRSRYNLGISCINLGAYREA
VSNFLTALSLQRKSRNQQQVPHPAISGNIWAALRIALSLMDQPELFQAANLGDLDVLLRA
FNLDP

Sequence of entity 2 (B), FASTA

>4EQF_2 Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (chains B)
SRLSSNL

Primary citation

Structure and stoichiometry of an accessory subunit TRIP8b interaction with hyperpolarization-activated cyclic nucleotide-gated channels. Bankston, J.R., Camp, S.S., Dimaio, F. et al. Proc Natl Acad Sci U S A (2012) 109:7899-7904. DOI 10.1073/pnas.1201997109 · PubMed

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