SAXSdb — 1h43

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1. Protein Identity and Related Structures Protein Identity & Related Structures

LACTOFERRIN

HOMO SAPIENS

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 20–353	Fragment：N-TERMINAL LOBE, RESIDUES 20-353 Mutation：YES	CO3 CARBONATE ION × 1 FE FE (III) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；HEPES, NACL, pH 8.00	Resolution 2.20 Å R-free 0.235

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1H43	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B0L RECOMBINANT HUMAN DIFERRIC LACTOFERRIN Deposited 1998-11-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 20–710（691 aa）	Mutation：A10T	FE FE (III) ION × 2 CO3 CARBONATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；DIALYSIS AGAINST 10MM SODIUM PHOSPHATE PH 8.0, CONTAINING 10% ETHANOL	Resolution 2.20 Å R-free 0.274
1BKA OXALATE-SUBSTITUTED DIFERRIC LACTOFERRIN Deposited 1996-04-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 20–711（692 aa）	Not recorded	FE FE (III) ION × 2 OXL OXALATE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.40 Å
1CB6 STRUCTURE OF HUMAN APOLACTOFERRIN AT 2.0 A RESOLUTION. Deposited 1999-03-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 20–710（691 aa） Fragment：UNP residues 20-710	Not recorded	CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；pH 7.8	Resolution 2.00 Å R-free 0.286
1DSN D60S N-TERMINAL LOBE HUMAN LACTOFERRIN Deposited 1995-12-13	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 21–353（333 aa） Fragment：N-TERMINAL LOBE RESIDUES 1 - 333	Mutation：D60S	FE FE (III) ION × 1 CO3 CARBONATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；pH 8.0	Resolution 2.05 Å
1EH3 R210K N-TERMINAL LOBE HUMAN LACTOFERRIN Deposited 2000-02-18	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 15–348（334 aa） Fragment：N-TERMINAL LOBE	Mutation：R210K	FE FE (III) ION × 1 CO3 CARBONATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions LIQUID DIFFUSION；pH 8；277 K；HEPES, NaCl, pH 8.0, LIQUID DIFFUSION, temperature 4K	Resolution 2.00 Å R-free 0.250
1FCK STRUCTURE OF DICERIC HUMAN LACTOFERRIN Deposited 2000-07-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 20–711（692 aa）	Not recorded	CO3 CARBONATE ION × 2 CE CERIUM (III) ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å R-free 0.257
1H44 R210L N-TERMINAL LOBE HUMAN LACTOFERRIN Deposited 2002-10-03	Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 20–353（334 aa） Fragment：N-TERMINAL LOBE, RESIDUES 20-353	Mutation：YES	FE FE (III) ION × 1 CO3 CARBONATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；HEPES, NACL, pH 8.00	Resolution 2.00 Å R-free 0.241
1H45 R210G N-TERMINAL LOBE HUMAN LACTOFERRIN Deposited 2002-10-03	Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 20–353（334 aa） Fragment：N-TERMINAL LOBE, RESIDUES 20-353	Mutation：YES	FE FE (III) ION × 1 CO3 CARBONATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；HEPES, NACL, pH 8.00	Resolution 1.95 Å R-free 0.248
1HSE H253M N TERMINAL LOBE OF HUMAN LACTOFERRIN Deposited 1996-12-11	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 21–347（327 aa） Fragment：N-TERMINAL HALF-MOLECULE	Mutation：H253M	FE FE (III) ION × 1 CO3 CARBONATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
1L5T Crystal Structure of a Domain-Opened Mutant (R121D) of the Human Lactoferrin N-lobe Refined From a Merohedrally-Twinned Crystal Form. Deposited 2002-03-07	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 21–352（332 aa） Fragment：RESIDUES 21-352	Mutation：R121D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 8；298 K；concentrated solution of the protein (50-80 mg mL-1), 0.01 M Tris-HCl, pH 8.0, 12% (v/v) isopropanol, MICRODIALYSIS, temperature 298K	Resolution 3.00 Å R-free 0.199
1L5T Crystal Structure of a Domain-Opened Mutant (R121D) of the Human Lactoferrin N-lobe Refined From a Merohedrally-Twinned Crystal Form. Deposited 2002-03-07	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 21–352（332 aa） Fragment：RESIDUES 21-352	Mutation：R121D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 8；298 K；concentrated solution of the protein (50-80 mg mL-1), 0.01 M Tris-HCl, pH 8.0, 12% (v/v) isopropanol, MICRODIALYSIS, temperature 298K	Resolution 3.00 Å R-free 0.199
1LCF CRYSTAL STRUCTURE OF COPPER-AND OXALATE-SUBSTITUTED HUMAN LACTOFERRIN AT 2.0 ANGSTROMS RESOLUTION Deposited 1994-01-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 22–711（690 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CU COPPER (II) ION × 2 CO3 CARBONATE ION × 1 OXL OXALATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
1LCT STRUCTURE OF THE RECOMBINANT N-TERMINAL LOBE OF HUMAN LACTOFERRIN AT 2.0 ANGSTROMS RESOLUTION Deposited 1993-06-19	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 21–353（333 aa）	Not recorded	FE FE (III) ION × 1 CO3 CARBONATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
1LFG Structure of diferric human lactoferrin Deposited 1992-02-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 22–711（690 aa）	Not recorded	FE FE (III) ION × 2 CO3 CARBONATE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
1LFH MOLECULAR REPLACEMENT SOLUTION OF THE STRUCTURE OF APOLACTOFERRIN, A PROTEIN DISPLAYING LARGE-SCALE CONFORMATIONAL CHANGE Deposited 1991-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 22–711（690 aa）	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å
1LFI METAL SUBSTITUTION IN TRANSFERRINS: THE CRYSTAL STRUCTURE OF HUMAN COPPER-LACTOFERRIN AT 2.1 ANGSTROMS RESOLUTION Deposited 1992-02-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 22–711（690 aa）	Not recorded	CU COPPER (II) ION × 2 CO3 CARBONATE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å
1LGB INTERACTION OF A LEGUME LECTIN WITH THE N2 FRAGMENT OF HUMAN LACTOTRANSFERRIN OR WITH THE ISOLATED BIANTENNARY GLYCOPEPTIDE: ROLE OF THE FUCOSE MOIETY Deposited 1994-01-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 111–269（159 aa）	Not recorded	MN MANGANESE (II) ION × 2 CA CALCIUM ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.30 Å
1LGB INTERACTION OF A LEGUME LECTIN WITH THE N2 FRAGMENT OF HUMAN LACTOTRANSFERRIN OR WITH THE ISOLATED BIANTENNARY GLYCOPEPTIDE: ROLE OF THE FUCOSE MOIETY Deposited 1994-01-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 111–269（159 aa）	Not recorded	MN MANGANESE (II) ION × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.30 Å
1N76 CRYSTAL STRUCTURE OF HUMAN SEMINAL LACTOFERRIN AT 3.4 A RESOLUTION Deposited 2002-11-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 22–711（690 aa）	Not recorded	NA SODIUM ION × 1 FE FE (III) ION × 2 CO3 CARBONATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 8；298 K；Tris-HCl, ethanol, pH 8.0, MICRODIALYSIS, temperature 298.0K	Resolution 3.40 Å R-free 0.266
1SQY Structure of human diferric lactoferrin at 2.5A resolution using crystals grown at pH 6.5 Deposited 2004-03-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 20–710（691 aa）	Not recorded	FE FE (III) ION × 2 CO3 CARBONATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 6.5；277 K；Ethanol, Tris-HCL, pH 6.5, MICRODIALYSIS, temperature 277K	Resolution 2.50 Å R-free 0.215
1U62 NMR structure analysis of the lactoferrin-based peptide FQWQRNIRKVR in complex with lipopolysaccharide Deposited 2004-07-29	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 39–49（11 aa） Fragment：LF11	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；303 K；Ionic strength (raw mmCIF value) 20；Pressure 1 NMR sample composition 2mM lacfotefficin; 20mM sodium phosphate buffer (pH=5.5); 95% H2O, 5% D2O \| 95% H2O/5% D2O	Resolution not provided
1VFD HUMAN LACTOFERRIN, N-TERMINAL LOBE MUTANT WITH ARG 121 REPLACED BY GLU (R121E) Deposited 1996-10-01	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 22–350（329 aa） Fragment：N-TERMINAL HALF-MOLECULE	Mutation：R121E	FE FE (III) ION × 1 CO3 CARBONATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.310
1VFE HUMAN LACTOFERRIN, N-TERMINAL LOBE MUTANT WITH ARG 121 REPLACED BY SER (R121S) Deposited 1996-10-01	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 22–353（332 aa） Fragment：N-TERMINAL HALF-MOLECULE	Mutation：R121S	FE FE (III) ION × 1 CO3 CARBONATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；50MM TRIS/HCL PH 8.0, 12% ISOPROPANOL	Resolution 2.30 Å R-free 0.270
1Z6V Human lactoferricin Deposited 2005-03-23	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 20–68（49 aa） Fragment：N-terminal peptide	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3；298 K；Ionic strength (raw mmCIF value) no salt added；Pressure ambient NMR sample composition 1mM lactoferricin \| 4:4:1 chloroform-d:methanol-d3:D2O	Resolution not provided
1Z6W Human Lactoferricin Deposited 2005-03-23	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 20–68（49 aa） Fragment：N-terminal peptide	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.5；298 K；Ionic strength (raw mmCIF value) no salt added；Pressure ambient NMR sample composition 1mM lactoferricin \| 90% H20, 10% D2O	Resolution not provided
2BJJ Structure of recombinant human lactoferrin produced in the milk of transgenic cows Deposited 2005-02-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain X 20–711（692 aa）	Not recorded	FE FE (III) ION × 2 CO3 CARBONATE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；5 MM SODIUM PHOSPHATE PH 8.5, 10% (V/V) ETHANOL	Resolution 2.40 Å R-free 0.231
2DP4 Crystal structure of the complex formed between proteinase K and a human lactoferrin fragment at 2.9 A resolution Deposited 2006-05-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain I 528–535（8 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；0.2M Ammonium actate, 0.1M sodium acetate, 30% PEG 4000, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.90 Å R-free 0.235
7N88 The cryoEM structure of LbpB from N. gonorrhoeae in complex with lactoferrin Deposited 2021-06-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 20–710（691 aa）	Not recorded	FE FE (III) ION × 2 BCT BICARBONATE ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å

26 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TRFL_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–334； UniProt 20–353

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1h43
Deposition date deposition_date	2002-10-02
Structure title title	R210E N-TERMINAL LOBE HUMAN LACTOFERRIN
Keywords keywords	METAL TRANSPORT, IRON TRANSPORT, METAL BINDING; METAL TRANSPORT
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	20.76 Å
Radius of gyration Rg (electron density) rg_electron	19.69 Å
Forward intensity I(0) i0	21025900.00
Molecular weight molecular_weight	34165.0 kDa
Excluded volume excluded_volume	42437 Å³
Envelope volume envelope_volume	50061 Å³
Hydration-shell volume shell_volume	21068 Å³
Envelope diameter envelope_diameter	68.0 Å
Shell Rg shell_rg	26.21 Å
Envelope Rg envelope_rg	19.90 Å
Shape Rg shape_rg	19.67 Å
Total Rg total_rg	20.60 Å
Total atoms total_atoms	2403
Residues n_residues	310
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	68.0 Å
Rg (real space) rg_real	20.67 Å
Rg uncertainty (real space) rg_real_error	0.38 Å
I(0) (real space) i0_real	2.1030e+07
I(0) uncertainty (real space) i0_real_error	2.8150e+05
Rg (reciprocal space) rg_reciprocal	20.69 Å
I(0) (reciprocal space) i0_reciprocal	21030000.0000
Solution quality estimate total_estimate	0.8895
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	24.6 Å
Skewness Skewness skewness	0.222
Kurtosis Kurtosis kurtosis	-0.438
Angular range angular_range	— – 0.3850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3888000.0000
Real-space data points n_real_points	70
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.859; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.982

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	LACTOFERRIN
Molecular weight formula_weight	37150.1 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2479

GRRRRSVQWCAVSQPEATKCFQWQRNMRRVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIEESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRK

来源 Source

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	CRICETULUS GRISEUS

Entity 2 Entity 2 non-polymer

Description description	CARBONATE ION
Molecular weight formula_weight	60.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	FE (III) ION
Molecular weight formula_weight	55.8 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	76

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1h43a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamily	c.94.1 — Periplasmic binding protein-like II
Family Family family	c.94.1.2 — Transferrin

CATH v4.4 (2 domains)

Domain ID domain_id	1h43A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	1h43A02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

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8. Citations (1)

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Unit-cell length a length_a	112.900 Å
Unit-cell length b length_b	57.900 Å
Unit-cell length c length_c	57.800 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	101.40 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2030
R_work r_work	0.2030
R_free r_free	0.2350

fit	/app/data/saxs_computation/h4/1h43/1h43.fit
pddf	/app/data/pr_computation/h4/1h43/1h43.pr.out
profile	/app/data/saxs_computation/h4/1h43/1h43.dat

R210E N-TERMINAL LOBE HUMAN LACTOFERRIN

1. Protein Identity and Related Structures Protein Identity & Related Structures

LACTOFERRIN

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction