1H6P: Dimeristion domain from human TRF2

Dimeristion domain from human TRF2. Determined by X-ray diffraction at 2.2 Å resolution. Released 5 Sept 2001.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
3,057
Mol. weight
47.36 kDa
Ligands
MG
Released
5 Sept 2001

Explore 1H6P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1H6P contains 20 α-helices and 0 β-strands across 2 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: 10 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix44-6926
α-helix73-8614
α-helix98-11114
α-helix128-14215
α-helix147-16721
α-helix171-18111
α-helix193-2019
α-helix214-22714
α-helix232-2343
α-helix235-24410
Chain B: 10 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix1046-106924
α-helix1073-108614
α-helix1097-111216
α-helix1128-114215
α-helix1147-116721
α-helix1171-118010
α-helix1193-12019
α-helix1214-122613
α-helix1232-12343
α-helix1235-12428

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Telomeric repeat binding factor 2A, Bprotein203HOMO SAPIENSQ15554 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1H6P_1 TELOMERIC REPEAT BINDING FACTOR 2 (chains A, B)
AGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQIRDIMQALLVRPLGKEHTVSRLLR
VMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTEAVVESSRKLVKEAAV
IICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNIIREKNLAHPVIQNFSYETFQQKML
RFLESHLDDAEPYLLTMAKKALK

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

Primary citation

Structure of the Trfh Dimerization Domain of the Human Telomere Proteins Trf1 and Trf2. Fairall, L., Chapman, L., Moss, H. et al. Mol Cell (2001) 8:351-361. DOI 10.1016/S1097-2765(01)00321-5 · PubMed

Other PDB entries of the same protein (UniProt Q15554 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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