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Crystal structure of PHF20L1 TUDOR1 in complex with K142ME1 DNMT1

Analyse Crystal structure of PHF20L1 TUDOR1 in complex with K142ME1 DNMT1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6L1F
Type: protein
Length: 73 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: The K142ME1 DNMT1 peptide; Phd finger protein 20-like protein 1
UniProt: P26358, A8MW92

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	The K142ME1 DNMT1 peptide	protein	6	0% helix, 0% strand	P26358
B	Phd finger protein 20-like protein 1	protein	67	4% helix, 43% strand	A8MW92

Interfaces

1 interface between chains.

A–B · 336 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

6L1F · Crystal structure of PHF20L1 Tudor1 in complex with K142me1 DNMT1 · the same entry in another collection · chain A against A, TM-score 1.00
A8MW92 · AlphaFold monomer V2.0 prediction for phd finger protein 20-like protein 1 (A8MW92) · a predicted model of the same protein · chain B against A, TM-score 0.96
P26358 · AlphaFold monomer V2.0 prediction for DNA (cytosine-5)-methyltransferase 1 (P26358) · a predicted model of the same protein · chain A against A, TM-score 0.66

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 P26358
Every structure of UniProt A8MW92
Elsewhere: RCSB PDB 6L1F · PDBe 6L1F · UniProt P26358 · UniProt A8MW92

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