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Crystal structure of the coiled coil domain of MURF1

Analyse Crystal structure of the coiled coil domain of MURF1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4M3L
Type: protein
Length: 228 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase TRIM63
EC: 6.3.2.-
UniProt: Q969Q1

Structure

x-ray diffraction · 4 distinct chains · 94% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase TRIM63 (EC 6.3.2.-)	protein	60	93% helix, 0% strand	Q969Q1
C	E3 ubiquitin-protein ligase TRIM63 (EC 6.3.2.-)	protein	57	95% helix, 0% strand	Q969Q1
B	E3 ubiquitin-protein ligase TRIM63 (EC 6.3.2.-)	protein	58	95% helix, 0% strand	Q969Q1
D	E3 ubiquitin-protein ligase TRIM63 (EC 6.3.2.-)	protein	53	94% helix, 0% strand	Q969Q1

Ligands and binding sites

GOL · Glycerol · additive · 11 copies · chains A, C, B, D
ACT · Acetate ion · additive · 9 copies · chains A, C, B, D
MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A, C

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

Interfaces

6 interfaces between chains.

B–D · 973 Å² buried · 8 hydrogen bonds · protein-protein
A–C · 849 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 709 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 469 Å² buried · 5 hydrogen bonds · protein-protein
C–B · 446 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4M3L · Crystal Structure of the coiled coil domain of MuRF1 · the same entry in another collection · chain D against D, TM-score 1.00
Q969Q1 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase TRIM63 (Q969Q1) · a predicted model of the same protein · chain B against A, TM-score 0.94

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 Q969Q1
Elsewhere: RCSB PDB 4M3L · PDBe 4M3L · UniProt Q969Q1

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