MolNFT v1 · #834 · protein

Apo ovotransferrin

1AIV: “Apo ovotransferrin”. X-ray diffraction, 2 ligands (NAG, NDG), 10 pockets (best druggability 0.77). MolNFT v1 #834 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1AIV
Type: protein
Length: 686 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ovotransferrin
UniProt: P02789
Ligands: NAG, NDG
Pockets: 10 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ovotransferrin	protein	686	27% helix, 11% strand	P02789

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · chains A

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

Pockets

10 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	1013	0.77	0.79	73	empty
2	56	0.74	0.99	18	empty
3	602	0.65	0.75	55	empty
4	177	0.58	0.82	32	empty
5	154	0.49	0.78	31	empty

Modifications

Observed in the structure: 15 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

1AIV · Apo ovotransferrin · 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 0.76

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 1AIV · PDBe 1AIV · UniProt P02789

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