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Hyperactive human ERO1

Analyse Hyperactive human ERO1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3AHQ
Type: protein
Length: 356 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ERO1-like protein alpha
EC: 1.8.4.-
UniProt: Q96HE7
Ligands: FAD
Pockets: 6 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ERO1-like protein alpha (EC 1.8.4.-)	protein	356	60% helix, 8% strand	Q96HE7

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	217	0.71	0.87	36	FAD
2	122	0.60	0.86	20	empty
3	310	0.55	0.76	37	empty
4	100	0.52	0.83	18	empty
5	135	0.44	0.76	23	empty

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

3AHQ · hyperactive human Ero1 · the same entry in another collection · chain A against A, TM-score 1.00
Q96HE7 · AlphaFold monomer V2.0 prediction for ERO1-like protein alpha (Q96HE7) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 Q96HE7
Elsewhere: RCSB PDB 3AHQ · PDBe 3AHQ · UniProt Q96HE7

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