1POG: Oct-1 pou homeodomain DNA-binding protein

Solution structure of the oct-1 pou-homeo domain determined by NMR and restrained molecular dynamics. Determined by solution NMR. Released 31 Jul 1995.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 532
Mol. weight: 8.19 kDa
Released: 31 Jul 1995

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

Secondary structure: helices and β-sheets

1POG contains 3 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: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	11-23	13
α-helix	28-38	11
α-helix	43-55	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Oct-1 pou homeodomain DNA-binding protein	A	protein	67	Homo sapiens	P14859 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1POG_1 OCT-1 POU HOMEODOMAIN DNA-BINDING PROTEIN (chains A)
RGSHMRRRKKRTSIETNIRVALEKSFLENQKPTSEEITMIADQLNMEKEVIRVWFCNRRQ
KEKRIDI

Primary citation

Solution structure of the Oct-1 POU homeodomain determined by NMR and restrained molecular dynamics. Cox, M., van Tilborg, P.J., de Laat, W. et al. J Biomol NMR (1995) 6:23-32. DOI 10.1007/BF00417488 · PubMed

Other PDB entries of the same protein (UniProt P14859 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1E3O 1.9 Å, Crystal structure of Oct-1 POU dimer bound to MORE
1GT0 2.6 Å, Crystal structure of a POU/HMG/DNA ternary complex
1HF0 2.7 Å, Crystal structure of the DNA-binding domain of Oct-1 bound to DNA as a dimer
1OCT 3.0 Å, Crystal structure of the oct-1 pou domain bound to an octamer site: DNA recognition with…
1CQT 3.2 Å, Crystal structure of a ternary complex containing an oca-B peptide, the oct-1 pou…
1O4X Ternary complex of the DNA binding domains of the OCT1 and SOX2 transcription factors…
1POU The solution structure of the oct-1 pou-specific domain reveals a striking similarity to…

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