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Ovotransferrin, N-terminal lobe, holo form, at 1.65 a resolution

Analyse Ovotransferrin, N-terminal lobe, holo form, at 1.65 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IEJ
Type: protein
Length: 329 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ovotransferrin
UniProt: P02789
Ligands: FE, CO3
Pockets: 4 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ovotransferrin	protein	329	35% helix, 22% strand	P02789

Ligands and binding sites

FE · Fe (III) ion · metal · chains A
CO3 · Carbonate ion · ion · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	196	0.81	0.96	39	empty
2	87	0.45	0.80	15	empty
3	95	0.35	0.74	20	empty
4	64	0.29	0.73	14	empty

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1IEJ · Ovotransferrin, N-terminal lobe, holo form, at 1.65 a resolution · the same entry in another collection · chain A against A, TM-score 1.00
P02789 · AlphaFold monomer V2.0 prediction for ovotransferrin (P02789) · 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 P02789
Elsewhere: RCSB PDB 1IEJ · PDBe 1IEJ · UniProt P02789

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