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Crystal structure of the STAC3 tandem SH3 domains - P269R, K329N

Analyse Crystal structure of the STAC3 tandem SH3 domains - P269R, K329N in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UY8
Type: protein
Length: 238 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SH3 and cysteine-rich domain-containing protein 3
UniProt: Q96MF2
Ligands: CL

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SH3 and cysteine-rich domain-containing protein 3	protein	123	11% helix, 40% strand	Q96MF2
B	SH3 and cysteine-rich domain-containing protein 3	protein	115	8% helix, 47% strand	Q96MF2

Ligands and binding sites

CL · Chloride ion · ion · chains B
EDO · 1,2-ethanediol · additive · 5 copies · 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 · 1094 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

6UY8 · Crystal structure of the STAC3 tandem SH3 domains - P269R, K329N · the same entry in another collection · chain A against A, TM-score 1.00
Q96MF2 · AlphaFold monomer V2.0 prediction for SH3 and cysteine-rich domain- containing protein 3… · a predicted model of the same protein · chain B against A, TM-score 0.98

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 Q96MF2
Elsewhere: RCSB PDB 6UY8 · PDBe 6UY8 · UniProt Q96MF2

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