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Crystal structure of the S. cerevisiae RTF1 histone modification domain mutant R126A

Analyse Crystal structure of the S. cerevisiae RTF1 histone modification domain mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5E8B
Type: protein
Length: 106 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA polymerase-associated protein RTF1
UniProt: P53064
Ligands: BEN, NA

Structure

x-ray diffraction · 2 distinct chains · 66% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA polymerase-associated protein RTF1	protein	54	67% helix, 4% strand	P53064
B	RNA polymerase-associated protein RTF1	protein	52	65% helix, 4% strand	P53064

Ligands and binding sites

BEN · Benzamidine · ligand · chains A, B
NA · Sodium ion · metal · 3 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

A–B · 167 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

5E8B · Crystal structure of the S. cerevisiae Rtf1 histone modification domain mutant R126A · the same entry in another collection · chain A against A, TM-score 1.00
P53064 · AlphaFold monomer V2.0 prediction for RNA polymerase-associated protein RTF1 (P53064) · a predicted model of the same protein · chain B against A, TM-score 0.97

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P53064
Elsewhere: RCSB PDB 5E8B · PDBe 5E8B · UniProt P53064

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