MolNFT v1 · #5410 · protein

R210K N-terminal lobe human lactoferrin

1EH3: “R210K N-terminal lobe human lactoferrin”. X-ray diffraction, 2 ligands (FE, CO3), 4 pockets (best druggability 0.79). MolNFT v1 #5410 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1EH3
Type: protein
Length: 324 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lactoferrin
UniProt: P02788
Ligands: FE, CO3
Pockets: 4 · best druggability 0.79

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lactoferrin	protein	324	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

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	145	0.79	0.96	28	empty
2	136	0.39	0.73	22	empty
3	66	0.35	0.77	19	empty
4	55	0.25	0.73	19	empty

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1EH3 · R210K N-terminal lobe 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 0.98

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 1EH3 · PDBe 1EH3 · UniProt P02788

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