MolNFT v1 · #10392 · protein

Ovotransferrin, C-terminal lobe, apo form

1IQ7: “Ovotransferrin, C-terminal lobe, apo form”. X-ray diffraction, 2 ligands (NAG, SO4), 2 pockets (best druggability 0.62). MolNFT v1 #10392 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1IQ7
Type: protein
Length: 341 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ovotransferrin
UniProt: P02789
Ligands: NAG, SO4
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ovotransferrin	protein	341	36% helix, 18% strand	P02789

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

2 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	510	0.62	0.75	54	SO4
2	64	0.30	0.74	17	empty

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

1IQ7 · Ovotransferrin, C-Terminal Lobe, Apo Form · 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 0.77

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 1IQ7 · PDBe 1IQ7 · UniProt P02789

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