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Crystal structure of the carboxy terminus of HOMER1

Analyse Crystal structure of the carboxy terminus of HOMER1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CVE
Type: protein
Length: 261 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Homer protein homolog 1
UniProt: Q9Z214

Structure

x-ray diffraction · 3 distinct chains · 96% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Homer protein homolog 1	protein	68	96% helix, 0% strand	Q9Z214
B, C	Homer protein homolog 1	protein	66	97% helix, 0% strand	Q9Z214
D	Homer protein homolog 1	protein	61	97% helix, 0% strand	Q9Z214

Interfaces

6 interfaces between chains.

A–B · 1079 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 1068 Å² buried · 7 hydrogen bonds · protein-protein
B–D · 785 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 776 Å² buried · 5 hydrogen bonds · protein-protein
A–D · 689 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

3CVE · Crystal Structure of the carboxy terminus of Homer1 · the same entry in another collection · chain A against A, TM-score 1.00
Q9Z214 · AlphaFold monomer V2.0 prediction for homer protein homolog 1 (Q9Z214) · a predicted model of the same protein · chain D against A, TM-score 0.96

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 Q9Z214
Elsewhere: RCSB PDB 3CVE · PDBe 3CVE · UniProt Q9Z214

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