4GO6: HCF-1 self-association sequence 1

Crystal structure of HCF-1 self-association sequence 1. Determined by X-ray diffraction at 2.7 Å resolution. Released 17 Oct 2012.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,295
Mol. weight: 60.68 kDa
Released: 17 Oct 2012

Explore 4GO6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4GO6 contains 9 α-helices and 45 β-strands across 4 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: 1 helix, 3 β-strands

Element	Residues	Length	Sheet
α-helix	363-365	3
β-strand	368-375	8	1
β-strand	380-385	6	1
β-strand	392-399	8	2

Chain B: 3 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	1813-1818	6	2
β-strand	1822-1825	4	1
β-strand	1827-1829	3	3
β-strand	1853-1855	3	3
α-helix	1856-1857	2
β-strand	1861-1870	10	2
β-strand	1873-1877	5	2
β-strand	1881-1884	4	2
α-helix	1885-1887	3
β-strand	1895-1902	8	4
β-strand	1905-1911	7	4
β-strand	1922-1929	8	5
β-strand	1946-1954	9	5
β-strand	1958-1962	5	4
α-helix	1963-1966	4
β-strand	1969	1	5
β-strand	1971	1	6
β-strand	1972-1973	2	5
β-strand	1977-1986	10	5
β-strand	1991	1	5
β-strand	1995-2000	6	5
β-strand	2015	1	5

Chain C: 1 helix, 3 β-strands

Element	Residues	Length	Sheet
α-helix	364-366	3
β-strand	371-375	5	7
β-strand	380-383	4	7
β-strand	392-399	8	6

Chain D: 4 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	1813-1818	6	6
β-strand	1822-1825	4	7
β-strand	1827-1828	2	8
β-strand	1829	1	6
β-strand	1854-1855	2	8
α-helix	1856-1857	2
β-strand	1861-1870	10	6
β-strand	1873-1874	2	6
α-helix	1876-1880	5
β-strand	1881-1884	4	6
β-strand	1895-1901	7	9
β-strand	1905-1911	7	9
β-strand	1922-1928	7	5
β-strand	1929	1	10
β-strand	1936	1	2
β-strand	1945-1954	10	5
β-strand	1958-1962	5	9
α-helix	1963-1966	4
β-strand	1969	1	10
α-helix	1970	1
β-strand	1971-1972	2	5
β-strand	1978-1986	9	5
β-strand	1991	1	5
β-strand	1995-2000	6	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
HCF N-terminal chain 1	A, C	protein	45	Homo sapiens	P51610 (AlphaFold model)
HCF C-terminal chain 1	B, D	protein	232	Homo sapiens	P51610 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>4GO6_1 HCF N-terminal chain 1 (chains A, C)
GSETEKPPPPARVQLVRANTNSLEVSWGAVATADSYLLQLQKYDI

Sequence of entity 2 (B, D), FASTA

>4GO6_2 HCF C-terminal chain 1 (chains B, D)
GSMKKENQWFDVGVIKGTNVMVTHYFLPPDDAVPSDDDLGTVPDYNQLKKQELQPGTAYK
FRVAGINACGRGPFSEISAFKTCLPGFPGAPCAIKISKSPDGAHLTWEPPSVTSGKIIEY
SVYLAIQSSQAGGELKSSTPAQLAFMRVYCGPSPSCLVQSSSLSNAHIDYTTKPAIIFRI
AARNEKGYGPATQVRWLQETSKDSSGTKPANKRPMSSPEMKSAPKKSKADGQ

Primary citation

HCF-1 self-association via an interdigitated Fn3 structure facilitates transcriptional regulatory complex formation. Park, J., Lammers, F., Herr, W. et al. Proc Natl Acad Sci U S A (2012) 109:17430-17435. DOI 10.1073/pnas.1208378109 · PubMed

Other PDB entries of the same protein (UniProt P51610 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4N39 1.76 Å, Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat…
4N3A 1.88 Å, Crystal Structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat…
5LWV 1.9 Å, Human OGT in complex with UDP and fused substrate peptide (HCF1)
6MA3 2.0 Å, Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat…
6MA4 2.0 Å, Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat…
6MA5 2.0 Å, Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat…
6MA2 2.1 Å, Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat…
4N3B 2.17 Å, Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1…
4N3C 2.55 Å, Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1…
6MA1 2.75 Å, Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat…

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