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Crystal structure of eash

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

PDB: 4NAO
Type: protein
Length: 282 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative oxygenase
UniProt: G8GV69
Ligands: AKG, NA, FE2
Pockets: 3 · best druggability 0.69

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative oxygenase	protein	282	28% helix, 24% strand	G8GV69

Ligands and binding sites

AKG · 2-oxoglutaric acid · ligand · chains A
NA · Sodium ion · metal · chains A
FE2 · Fe (II) ion · metal · chains A
P6G · Hexaethylene glycol · additive · 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	495	0.69	0.79	55	AKG, FE2
2	53	0.40	0.82	15	empty
3	53	0.36	0.79	18	NA

Compared structures

4NAO · Crystal structure of EasH · the same entry in another collection · chain A against A, TM-score 1.00
G8GV69 · AlphaFold monomer V2.0 prediction for dioxygenase eash (G8GV69) · 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 G8GV69
Elsewhere: RCSB PDB 4NAO · PDBe 4NAO · UniProt G8GV69

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