Current Protein Identity:O77811 New Search
Main Difference Dimensions in This Set
Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1B1X STRUCTURE OF DIFERRIC MARE LACTOFERRIN AT 2.62A RESOLUTION Deposited 1998-11-24 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 7–695(689 aa)
Not recorded FE FE (III) ION × 2 CO3 CARBONATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5;40MG/ML PROTEIN IN 10MM TRIS HCL, PH 8.5, MICRODIALYSED AGA AT 6 DEGREES CELSIUS
Resolution 2.62 Å R-free 0.264
1B7U Structure of Mare Apolactoferrin: the N and C Lobes are in the Closed Form Deposited 1999-01-01 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 7–695(689 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 8.5;pH 8.5, VAPOR DIFFUSION, HANGING DROP
Resolution 3.80 Å R-free 0.300
1B7Z STRUCTURE OF OXALATE SUBSTITUTED DIFERRIC MARE LACTOFERRIN FROM COLOSTRUM Deposited 1999-01-26 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 7–695(689 aa)
Not recorded FE FE (III) ION × 2 OXL OXALATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5;30 MG/ML PROTEIN IN 0.025M TRIS-HCL DIALYZED AGAINST SAME BUFFER MADE AS 10% (V/V) ETHANOL AT PH 8.5
Resolution 2.70 Å R-free 0.274
1F9B MELANIN PROTEIN INTERACTION: X-RAY STRUCTURE OF THE COMPLEX OF MARE LACTOFERRIN WITH MELANIN MONOMERS Deposited 2000-07-10 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–695(695 aa)
Not recorded FE FE (III) ION × 2 BCT BICARBONATE ION × 2 3ID 3H-INDOLE-5,6-DIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions MICRODIALYSIS;pH 5;277 K;20mM Tris-Hcl, pH 5.0 concentration 50 mg/ml 10% ethanol soaked for 12hours in buffer containing DOPA, MICRODIALYSIS, temperature 4K
Resolution 2.70 Å R-free 0.287
1I6B STRUCTURE OF EQUINE APOLACTOFERRIN AT 3.2 A RESOLUTION USING CRYSTALS GROWN AT 303K Deposited 2001-03-02 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 7–695(689 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions MICRODIALYSIS;pH 8;303 K;ethanol, pH 8.0, MICRODIALYSIS, temperature 303K
Resolution 3.20 Å R-free 0.291
1QJM Crystal Structure of a Complex of Lactoferrin with a Lanthanide Ion (SM3+) at 3.4 Angstrom Resolution Deposited 1999-06-27 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 7–695(689 aa)
Not recorded SM SAMARIUM (III) ION × 2 CO3 CARBONATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8;277 K;PROTEIN SOLUTION WITH A CONCENTRATION OF 40MG/ML IN 0.025M TRIS-HCL WAS EQUILIBRATED AGAINST THE SAME BUFFER CONTAINING 10% (V/V) ETHANOL AT PH 8.0 AT 4 DEGREE.
Resolution 3.40 Å R-free 0.316
3CR9 Crystal structure of the complex of Lactoferrin with 6-(Hydroxymethyl)oxane-2,3,4,5-tetrol at 3.49 A resolution Deposited 2008-04-05 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 7–695(689 aa)
Not recorded GLC alpha-D-glucopyranose × 1 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;50mM Tris, pH 8, 21% Ethanol, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 3.49 Å R-free 0.226