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Crystal structure of the native BICC1 SAM domain R924E mutant

Analyse Crystal structure of the native BICC1 SAM domain R924E mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RQN
Type: protein
Length: 184 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein bicaudal C homolog 1
UniProt: Q9H694
Ligands: ZN

Structure

x-ray diffraction · 3 distinct chains · 69% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein bicaudal C homolog 1	protein	61	69% helix, 0% strand	Q9H694
B	Protein bicaudal C homolog 1	protein	61	67% helix, 0% strand	Q9H694
C	Protein bicaudal C homolog 1	protein	62	71% helix, 0% strand	Q9H694

Ligands and binding sites

ZN · Zinc ion · metal · chains A, B

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

Interfaces

2 interfaces between chains.

A–B · 340 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 291 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

4RQN · Crystal structure of the native BICC1 SAM Domain R924E mutant · the same entry in another collection · chain A against A, TM-score 1.00
Q9H694 · AlphaFold monomer V2.0 prediction for protein bicaudal C homolog 1 (Q9H694) · a predicted model of the same protein · chain B against A, TM-score 0.95

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 Q9H694
Elsewhere: RCSB PDB 4RQN · PDBe 4RQN · UniProt Q9H694

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