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MORC3 cw in complex with histone H3K4ME1

Analyse MORC3 cw in complex with histone H3K4ME1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5SVY
Type: protein
Length: 61 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Morc family cw-type zinc finger protein 3; H3K4ME1
UniProt: Q14149
Ligands: ZN

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Morc family cw-type zinc finger protein 3	protein	50	12% helix, 18% strand	Q14149
B	H3K4ME1	protein	11	0% helix, 36% strand	—

Ligands and binding sites

ZN · Zinc ion · metal · chains A
ACT · Acetate ion · additive · 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 · 729 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

5SVY · MORC3 CW in complex with histone H3K4me1 · the same entry in another collection · chain A against A, TM-score 1.00
Q14149 · AlphaFold monomer V2.0 prediction for morc family cw-type zinc finger protein 3 (Q14149) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 Q14149
Elsewhere: RCSB PDB 5SVY · PDBe 5SVY · UniProt Q14149

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