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The structure of artemis variant H35D

Analyse The structure of artemis variant H35D in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7AGI
Type: protein
Length: 359 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein artemis
EC: 3.1.-.-
UniProt: Q96SD1
Ligands: ZN
Pockets: 4 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein artemis (EC 3.1.-.-)	protein	359	28% helix, 24% strand	Q96SD1

Ligands and binding sites

ZN · Zinc ion · metal · chains A
EDO · 1,2-ethanediol · additive · 8 copies · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	291	0.68	0.83	49	empty
2	241	0.59	0.79	29	empty
3	81	0.30	0.72	19	EDO
4	55	0.27	0.73	17	empty

Compared structures

7AGI · The structure of Artemis variant H35D · the same entry in another collection · chain A against A, TM-score 1.00
Q96SD1 · AlphaFold monomer V2.0 prediction for protein artemis (Q96SD1) · a predicted model of the same protein · chain A 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 Q96SD1
Elsewhere: RCSB PDB 7AGI · PDBe 7AGI · UniProt Q96SD1

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