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H253M N terminal lobe of human lactoferrin

Analyse H253M N terminal lobe of human lactoferrin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HSE
Type: protein
Length: 317 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lactoferrin
UniProt: P02788
Ligands: FE, CO3
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lactoferrin	protein	317	33% helix, 21% strand	P02788

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

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	323	0.78	0.89	42	empty
2	53	0.27	0.74	10	empty

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1HSE · H253M N terminal lobe of human lactoferrin · the same entry in another collection · chain A against A, TM-score 1.00
P02788 · AlphaFold monomer V2.0 prediction for lactotransferrin (P02788) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 P02788
Elsewhere: RCSB PDB 1HSE · PDBe 1HSE · UniProt P02788

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