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Crystal structure of the EFC/F-bar domain of human PACSIN2/SYNDAPIN II (2.7 a)

Analyse Crystal structure of the EFC/F-bar domain of human PACSIN2/SYNDAPIN II (2.7 a) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ACO
Type: protein
Length: 568 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein kinase C and casein kinase substrate in neurons protein 2
UniProt: Q9UNF0
Ligands: CA

Structure

x-ray diffraction · 1 distinct chain · 79% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein kinase C and casein kinase substrate in neurons protein 2	protein	284	79% helix, 1% strand	Q9UNF0

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A

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

Interfaces

1 interface between chains.

A–B · 4159 Å² buried · 42 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified (engineered).

Compared structures

3ACO · Crystal structure of the EFC/F-BAR domain of human PACSIN2/Syndapin II (2.7 A) · the same entry in another collection · chain A against A, TM-score 1.00
Q9UNF0 · AlphaFold monomer V2.0 prediction for protein kinase C and casein kinase substrate in… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9UNF0
Elsewhere: RCSB PDB 3ACO · PDBe 3ACO · UniProt Q9UNF0

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