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Crystal structure of protein arginine deiminase 2 (F221/222A, 10 mm CA2+)

Analyse Crystal structure of protein arginine deiminase 2 (F221/222A, 10 mm CA2+) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4N2C
Type: protein
Length: 645 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein-arginine deiminase type-2
EC: 3.5.3.15
UniProt: Q9Y2J8
Ligands: CA
Pockets: 3 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein-arginine deiminase type-2 (EC 3.5.3.15)	protein	645	15% helix, 36% strand	Q9Y2J8

Ligands and binding sites

CA · Calcium ion · metal · 6 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	231	0.53	0.77	32	empty
2	53	0.46	0.84	19	empty
3	58	0.34	0.78	17	empty

Compared structures

4N2C · Crystal structure of Protein Arginine Deiminase 2 (F221/222A, 10 mM Ca2+) · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y2J8 · AlphaFold monomer V2.0 prediction for protein-arginine deiminase type-2 (Q9Y2J8) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9Y2J8
Elsewhere: RCSB PDB 4N2C · PDBe 4N2C · UniProt Q9Y2J8

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