Research workbench

Structure of mammalian NEIL2 from monodelphis domestica

Analyse Structure of mammalian NEIL2 from monodelphis domestica in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6VJI
Type: protein
Length: 508 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nei like DNA glycosylase 2
UniProt: F7AMK3
Ligands: ZN
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nei like DNA glycosylase 2	protein	255	27% helix, 26% strand	F7AMK3
B	Nei like DNA glycosylase 2	protein	253	27% helix, 24% strand	F7AMK3

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	590	0.65	0.76	55	empty
2	468	0.64	0.77	56	empty
3	274	0.63	0.80	34	empty
4	68	0.34	0.76	14	empty

Interfaces

1 interface between chains.

A–B · 1338 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

6VJI · Structure of mammalian NEIL2 from Monodelphis domestica · the same entry in another collection · chain A against A, TM-score 1.00

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 F7AMK3
Elsewhere: RCSB PDB 6VJI · PDBe 6VJI · UniProt F7AMK3

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.