SAXSdb — 1vfd

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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 22–350	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 experimental conditions	Resolution 2.50 Å R-free 0.310

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 1VFD	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 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 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
1H43 R210E N-TERMINAL LOBE HUMAN LACTOFERRIN Deposited 2002-10-02	Different construct Different mutation/modification Different experimental conditions 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	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
1H44 R210L N-TERMINAL LOBE HUMAN LACTOFERRIN Deposited 2002-10-03	Different construct Different mutation/modification Different experimental conditions 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 construct Different mutation/modification Different experimental conditions 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 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 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 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 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 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 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 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 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
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 2–330； UniProt 22–350

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	1vfd
Deposition date deposition_date	1996-10-01
Structure title title	HUMAN LACTOFERRIN, N-TERMINAL LOBE MUTANT WITH ARG 121 REPLACED BY GLU (R121E)
Keywords keywords	TRANSFERRIN, IRON TRANSPORT, GLYCOPROTEIN, METAL-BINDING; IRON 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	20.65 Å
Radius of gyration Rg (electron density) rg_electron	19.54 Å
Forward intensity I(0) i0	22650000.00
Molecular weight molecular_weight	35596.0 kDa
Excluded volume excluded_volume	44261 Å³
Envelope volume envelope_volume	52043 Å³
Hydration-shell volume shell_volume	21911 Å³
Envelope diameter envelope_diameter	68.4 Å
Shell Rg shell_rg	26.23 Å
Envelope Rg envelope_rg	19.75 Å
Shape Rg shape_rg	19.51 Å
Total Rg total_rg	20.49 Å
Total atoms total_atoms	2505
Residues n_residues	321
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	68.3 Å
Rg (real space) rg_real	20.55 Å
Rg uncertainty (real space) rg_real_error	0.33 Å
I(0) (real space) i0_real	2.2650e+07
I(0) uncertainty (real space) i0_real_error	2.6690e+05
Rg (reciprocal space) rg_reciprocal	20.56 Å
I(0) (reciprocal space) i0_reciprocal	22650000.0000
Solution quality estimate total_estimate	0.8841
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	67.3 Å
Skewness Skewness skewness	0.214
Kurtosis Kurtosis kurtosis	-0.389
Angular range angular_range	— – 0.3850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	5142000.0000
Real-space data points n_real_points	70
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.830; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.998

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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	36593.4 kDa
Mutation mutation	R121E
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	2589

GRRRSVQWCAVSQPEATKCFQWQRNMRRVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRETAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQN

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	Cricetinae

Entity 2 Entity 2 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 3 Entity 3 non-polymer

Description description	CARBONATE ION
Molecular weight formula_weight	60.0 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	84

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1vfda_
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	1vfdA01
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	1vfdA02
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 (2)

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Unit-cell length a length_a	98.100 Å
Unit-cell length b length_b	78.900 Å
Unit-cell length c length_c	113.600 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.2040
R_free r_free	0.3100

fit	/app/data/saxs_computation/vf/1vfd/1vfd.fit
pddf	/app/data/pr_computation/vf/1vfd/1vfd.pr.out
profile	/app/data/saxs_computation/vf/1vfd/1vfd.dat

HUMAN LACTOFERRIN, N-TERMINAL LOBE MUTANT WITH ARG 121 REPLACED BY GLU (R121E)