1G6G: N-terminal fha domain from S. Cerevisiae RAD53P

X-ray structure of the N-terminal fha domain from S. Cerevisiae RAD53P in complex with a phosphothreonine peptide at 1.6 a resolution. Determined by X-ray diffraction at 1.6 Å resolution. Released 13 Dec 2000.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 2,564
Mol. weight: 31.18 kDa
Released: 13 Dec 2000

Explore 1G6G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1G6G contains 10 α-helices and 22 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: 4 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	31-38	8	1
β-strand	46-50	5	1
α-helix	52-57	6
β-strand	64-69	6	2
β-strand	76-77	2	2
β-strand	89-93	5	2
β-strand	99-103	5	2
β-strand	110-111	2	1
β-strand	114-115	2	1
α-helix	116-117	2
β-strand	122-123	2	2
β-strand	129-132	4	1
α-helix	137-139	3
β-strand	141-147	7	1
α-helix	149-154	6

Chain B: 4 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	34-38	5	3
β-strand	46-48	3	3
α-helix	52-57	6
β-strand	62-69	8	4
β-strand	76-77	2	4
β-strand	89-94	6	4
β-strand	99-103	5	4
β-strand	109-111	3	3
β-strand	114-115	2	3
α-helix	116-117	2
β-strand	122-123	2	4
β-strand	129-132	4	3
α-helix	137-139	3
β-strand	141-147	7	3
α-helix	149-153	5

Chain E: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3

Chain F: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-8	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein kinase RAD53	A, B	protein	127	Saccharomyces cerevisiae	P22216 (AlphaFold model)
Ser-leu-glu-val-tpo-glu-ala-aspala-thr-phe-ala-lys	E, F	protein	13

Sequence of entity 1 (A, B), FASTA

>1G6G_1 PROTEIN KINASE RAD53 (chains A, B)
GENIVCRVICTTGQIPIRDLSADISQVLKEKRSIKKVWTFGRNPACDYHLGNISRLSNKH
FQILLGEDGNLLLNDISTNGTWLNGQKVEKNSNQLLSQGDEITVGVGVESDILSLVIFIN
DKFKQCL

Sequence of entity 2 (E, F), FASTA

>1G6G_2 SER-LEU-GLU-VAL-TPO-GLU-ALA-ASPALA-THR-PHE-ALA-LYS (chains E, F)
SLEVTEADATFAK

Primary citation

The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms. Durocher, D., Taylor, I.A., Sarbassova, D. et al. Mol Cell (2000) 6:1169-1182. DOI 10.1016/S1097-2765(00)00114-3 · PubMed

Other PDB entries of the same protein (UniProt P22216 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5T2S 2.4 Å, Structure of the FHA1 domain of Rad53 bound simultaneously to the BRCT domain of Dbf4…
4PDP 2.59 Å, Crystal structure of Rad53 kinase domain and SCD2
6C4U 2.6 Å, Engineered FHA with Myc-pTBD peptide
5T2F 2.66 Å, Structure of the FHA1 domain of Rad53 bound to the BRCT domain of Dbf4
5XZW 2.8 Å, Crystal structure of Rad53 1-466
4PDS 2.9 Å, Crystal structure of Rad53 kinase domain and SCD2 in complex with AMPPNP
2YGV 2.94 Å, Conserved N-terminal domain of the yeast Histone Chaperone Asf1 in complex with the…
5XZV 3.1 Å, Crystal structure of Rad53 1-466 in complex with AMP-PNP
1DMZ A refined NMR structure of a new phophopeptide-binding domain containing the FHA2 of RAD53
1FHQ Refined solution structure of the FHA2 domain of RAD53
1FHR Solution structure of the FHA2 domain of RAD53 complexed with a phosphotyrosyl peptide
1G3G NMR structure of the FHA1 domain of yeast RAD53

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