SAXSdb — 8a60

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

Ferrichrome outer membrane transporter/phage receptor

Escherichia coli K-12

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 34–747	Not recorded	Lytic conversion lipoprotein × 1 （Q38162）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；12-16% PEG 4000 0.4 M sodium isothiocyanate 0.1 M sodium acetate	Resolution 3.37 Å R-free 0.307

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 8A60	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BY3 FHUA FROM E. COLI Deposited 1998-10-22	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 34–747（714 aa）	Not recorded	OES N-OCTYL-2-HYDROXYETHYL SULFOXIDE × 7	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；PROTEIN WAS CRYSTALLIZED FROM 33% PEG2000, 0.45 M NACL, 0.15 M NAPI (PH 6.2) AND 0.5% N-OCTYL-2-HYDROXYETHYLSULFOXIDE	Resolution 2.74 Å R-free 0.244
1FCP FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI IN COMPLEX WITH BOUND FERRICHROME-IRON Deposited 1998-10-14	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 52–747（696 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	NI NICKEL (II) ION × 2 LIL 2-TRIDECANOYLOXY-PENTADECANOIC ACID × 2 AAE ACETOACETIC ACID × 1 LIM 3-OXO-PENTADECANOIC ACID × 1 EA2 AMINOETHANOLPYROPHOSPHATE × 1 FCI FERRICROCIN-IRON × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.4；100MM NA-CACODYLATE, PH 6.4, 12.5% PEG2000 MME, 20% GLYCEROL, 3% PEG200	Resolution 2.70 Å R-free 0.281
1FI1 FhuA in complex with lipopolysaccharide and rifamycin CGP4832 Deposited 2000-08-03	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 52–747（696 aa）	Mutation：HEXAHISTIDINE TAG PLUS FIVE LINKER RESIDUES HAVE BEEN GENETICALLY INSERTED AFTER RESIDUE 405 OF THE MATURE SEQUENCE	FTT 3-HYDROXY-TETRADECANOIC ACID × 6 PO4 PHOSPHATE ION × 2 NI NICKEL (II) ION × 1 NA SODIUM ION × 1 MG MAGNESIUM ION × 1 DPO DIPHOSPHATE × 2 RIF RIFAMYCIN CGP 4832 × 1 DDQ DECYLAMINE-N,N-DIMETHYL-N-OXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；291 K；100 mM sodium cacodylate, 12% PEG 2,000 MME, 3% PEG 200, 1% cis-inositol, 20% glycerol, 1 mM rifamycin CGP 4832, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.90 Å R-free 0.275
1QFF E. COLI FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) IN COMPLEX WITH BOUND FERRICHROME-IRON Deposited 1999-04-10	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 34–747（714 aa）	Mutation：SER-SER-HIS-HIS-HIS-HIS-HIS-HIS-GLY-SER-SER AFFINITY TAG Non-standard monomer：Yes (specific site not provided by mmCIF)	PO4 PHOSPHATE ION × 2 FTT 3-HYDROXY-TETRADECANOIC ACID × 4 DAO LAURIC ACID × 1 MYR MYRISTIC ACID × 1 DPO DIPHOSPHATE × 1 EAP 2-AMINO-VINYL-PHOSPHATE × 1 FCI FERRICROCIN-IRON × 1 DDQ DECYLAMINE-N,N-DIMETHYL-N-OXIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.4；pH 6.4	Resolution 2.70 Å R-free 0.276
1QFG E. COLI FERRIC HYDROXAMATE RECEPTOR (FHUA) Deposited 1999-04-10	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 34–747（714 aa）	Mutation：YES	NI NICKEL (II) ION × 1 PO4 PHOSPHATE ION × 2 FTT 3-HYDROXY-TETRADECANOIC ACID × 4 DAO LAURIC ACID × 1 MYR MYRISTIC ACID × 1 DDQ DECYLAMINE-N,N-DIMETHYL-N-OXIDE × 3 DPO DIPHOSPHATE × 2 GOL GLYCEROL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；290 K；100MM SODIUM CACODYLATE (PH 6.4), 12.5% PEG 2000 MONOMETHYLETHER, 20% GLYCEROL, 1% CIS-INOSITOL, 3% PEG 200, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 2.50 Å R-free 0.271
1QJQ FERRIC HYDROXAMATE RECEPTOR FROM ESCHERICHIA COLI (FHUA) Deposited 1999-06-29	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 34–438（405 aa） Chain A 439–747（309 aa）	Mutation：YES Mutation：YES	FTT 3-HYDROXY-TETRADECANOIC ACID × 6 DPO DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 NI NICKEL (II) ION × 1 PFC PHENYLFERRICROCIN-IRON × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.4；100MM SODIUM CACODYLATE (PH 6.4), 14.5% PEG 2000 MONOMETHYLETHER, 20% GLYCEROL, 3% PEG 200, 1 MM PHENYLFERRICROCIN-IRON	Resolution 2.95 Å R-free 0.278
1QKC ESCHERICHIA COLI FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) IN COMPLEX DELTA TWO-ALBOMYCIN Deposited 1999-07-18	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 34–438（405 aa） Chain A 439–747（309 aa）	Mutation：YES Mutation：YES	FTT 3-HYDROXY-TETRADECANOIC ACID × 6 DPO DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 NI NICKEL (II) ION × 1 ALB DELTA-2-ALBOMYCIN A1 × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.4；100 MM SODIUM CACODYLATE (PH 6.4), 14.0% POLYETHYLGLYCOL 2000 MONOMETHYLETHER, 20% GLYCEROL, 3% POLYETHYLGLYCOL 200, 1% CIS-INOSITOL, 0.3 MM DELTA TWO ALBOMYCIN	Resolution 3.10 Å R-free 0.283
2FCP FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI Deposited 1998-10-15	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 34–747（714 aa）	Not recorded	NI NICKEL (II) ION × 2 LIL 2-TRIDECANOYLOXY-PENTADECANOIC ACID × 2 AAE ACETOACETIC ACID × 1 LIM 3-OXO-PENTADECANOIC ACID × 1 EA2 AMINOETHANOLPYROPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.4；100MM NA-CACODYLATE, PH 6.4, 12.5% PEG2000 MME, 20% GLYCEROL, 1% CIS-INOSITOL, 3% PEG200	Resolution 2.50 Å R-free 0.283
2GRX Crystal structure of TonB in complex with FhuA, E. coli outer membrane receptor for ferrichrome Deposited 2006-04-25	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 34–758（725 aa）	Not recorded	PO4 PHOSPHATE ION × 1 FTT 3-HYDROXY-TETRADECANOIC ACID × 4 DPO DIPHOSPHATE × 1 DAO LAURIC ACID × 1 EAP 2-AMINO-VINYL-PHOSPHATE × 1 FCI FERRICROCIN-IRON × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；8% polyethylene glycol 4000, 50 mM MES (pH 6.0), 75 mM NaCl, 5% glycerol, 0.7% C8E4, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.30 Å R-free 0.329
2GRX Crystal structure of TonB in complex with FhuA, E. coli outer membrane receptor for ferrichrome Deposited 2006-04-25	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 34–758（725 aa）	Not recorded	PO4 PHOSPHATE ION × 1 FTT 3-HYDROXY-TETRADECANOIC ACID × 4 DPO DIPHOSPHATE × 1 DAO LAURIC ACID × 1 EAP 2-AMINO-VINYL-PHOSPHATE × 1 FCI FERRICROCIN-IRON × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；8% polyethylene glycol 4000, 50 mM MES (pH 6.0), 75 mM NaCl, 5% glycerol, 0.7% C8E4, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.30 Å R-free 0.329
4CU4 FhuA from E. coli in complex with the lasso peptide microcin J25 (MccJ25) Deposited 2014-03-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 53–438（386 aa） Fragment：RESIDUES 53-747 Chain A 439–747（309 aa） Fragment：RESIDUES 53-747	Not recorded	FTT 3-HYDROXY-TETRADECANOIC ACID × 4 DAO LAURIC ACID × 1 MYR MYRISTIC ACID × 1 LDA LAURYL DIMETHYLAMINE-N-OXIDE × 20 3PH 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE × 1 DPO DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；20 MM TRIS PH 7.5, 120 MM LITHIUM SULFATE, 100 MM SODIUM CITRATE PH 5, 20 % PEG300	Resolution 2.30 Å R-free 0.255
8A8C T5 phage receptor-binding protein pb5 bound to ferrichrome transporter FhuA Deposited 2022-06-22	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 34–747（714 aa）	Not recorded	LU9 [(2R,3S,4R,5R,6R)-2-[[(2R,4R,5R,6R)-6-[(1R)-1,2-bis(oxidanyl)ethyl]-4-[(2R,4R,5R,6R)-6-[(1R)-1,2-bis(oxidanyl)ethyl]-2-carboxy-4,5-bis(oxidanyl)oxan-2-yl]oxy-2-carboxy-5-oxidanyl-oxan-2-yl]oxymethyl]-5-[[(3R)-3-dodecanoyloxytetradecanoyl]amino]-4-(3-nonanoyloxypropanoyloxy)-6-[[(2R,3S,4R,5R,6R)-3-oxidanyl-4-[(3S)-3-oxidanyltetradecanoyl]oxy-5-[[(3R)-3-oxidanyltridecanoyl]amino]-6-phosphonatooxy-oxan-2-yl]methoxy]oxan-3-yl] phosphate × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
8B14 T5 Receptor Binding Protein pb5 in complex with its E. coli receptor FhuA Deposited 2022-09-09	Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 34–747（714 aa）	Mutation：Presence of an Histag after P405, added residues : SHHHHHHGS	DDQ DECYLAMINE-N,N-DIMETHYL-N-OXIDE × 1 LU9 [(2R,3S,4R,5R,6R)-2-[[(2R,4R,5R,6R)-6-[(1R)-1,2-bis(oxidanyl)ethyl]-4-[(2R,4R,5R,6R)-6-[(1R)-1,2-bis(oxidanyl)ethyl]-2-carboxy-4,5-bis(oxidanyl)oxan-2-yl]oxy-2-carboxy-5-oxidanyl-oxan-2-yl]oxymethyl]-5-[[(3R)-3-dodecanoyloxytetradecanoyl]amino]-4-(3-nonanoyloxypropanoyloxy)-6-[[(2R,3S,4R,5R,6R)-3-oxidanyl-4-[(3S)-3-oxidanyltetradecanoyl]oxy-5-[[(3R)-3-oxidanyltridecanoyl]amino]-6-phosphonatooxy-oxan-2-yl]methoxy]oxan-3-yl] phosphate × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8.5 cryo-EM vitrification conditions Cryogen ETHANE；3.5 microliters of the FhuA-pb5 complex were deposited on a freshly glow discharged (25 mA, 30 sec) Cu/Rh 400 mesh Quantifoil R 2/1 EM grids and flash-frozen in nitrogen-cooled liquid ethane using a ThermoFisher Mark IV Vitrobot device (100% humidity, 293.15K, 2s blotting time, blot force 1).	Resolution 2.60 Å

12 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FHUA_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–716； UniProt 34–747

Lytic conversion lipoprotein

Escherichia phage T5

UniProt Q38162

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 1–77	Not recorded	Ferrichrome outer membrane transporter/phage receptor × 1 （P06971）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；12-16% PEG 4000 0.4 M sodium isothiocyanate 0.1 M sodium acetate	Resolution 3.37 Å R-free 0.307

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 8A60	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7QJF Llp mutant C1G, lytic conversion lipoprotein of phage T5 Deposited 2021-12-16	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 17–77（61 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；303 K；Ionic strength (raw mmCIF value) 75；Pressure 1 NMR sample composition 25 mM no Tris, 75 mM no NaCl, 1.024 mM 13C 15N Sol-Llp, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	LLP_BPT5
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–77； UniProt 1–77

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	8a60
Deposition date deposition_date	2022-06-16
Structure title title	Crystal structure of FhuA in complex with the superinfection exclusion lipoprotein Llp
Keywords keywords	Outer membrane TonB-dependent transporter FhuA Bacteriophage T5 Superinfection exclusion E. coli, MEMBRANE PROTEIN; MEMBRANE PROTEIN
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	26.84 Å
Radius of gyration Rg (electron density) rg_electron	26.14 Å
Forward intensity I(0) i0	111564000.00
Molecular weight molecular_weight	82154.0 kDa
Excluded volume excluded_volume	102040 Å³
Envelope volume envelope_volume	122830 Å³
Hydration-shell volume shell_volume	38010 Å³
Envelope diameter envelope_diameter	96.6 Å
Shell Rg shell_rg	34.82 Å
Envelope Rg envelope_rg	26.19 Å
Shape Rg shape_rg	26.15 Å
Total Rg total_rg	26.93 Å
Total atoms total_atoms	5804
Residues n_residues	739
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	97.3 Å
Rg (real space) rg_real	26.74 Å
Rg uncertainty (real space) rg_real_error	0.71 Å
I(0) (real space) i0_real	1.1160e+08
I(0) uncertainty (real space) i0_real_error	1.7300e+06
Rg (reciprocal space) rg_reciprocal	26.77 Å
I(0) (reciprocal space) i0_reciprocal	111600000.0000
Solution quality estimate total_estimate	0.7539
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	33.0 Å
Skewness Skewness skewness	0.297
Kurtosis Kurtosis kurtosis	-0.221
Angular range angular_range	— – 0.2950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	28150000.0000
Real-space data points n_real_points	60
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.608; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Ferrichrome outer membrane transporter/phage receptor
Molecular weight formula_weight	79035.1 kDa
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	5804

SMAVEPKEDTITVTAAPAPQESAWGPAATIAARQSATGTKTDTPIQKVPQSISVVTAEEMALHQPKSVKEALSYTPGVSVGTRGASNTYDHLIIRGFAAEGQSQNNYLNGLKLQGNFYNDAVIDPYMLERAEIMRGPVSVLYGKSSPGGLLNMVSKRPTTEPLKEVQFKAGTDSLFQTGFDFSDSLDDDGVYSYRLTGLARSANAQQKGSEEQRYAIAPAFTWRPDDKTNFTFLSYFQNEPETGYYGWLPKEGTVEPLPNGKRLPTDFNEGAKNNTYSRNEKMVGYSFDHEFNDTFTVRQNLRFAENKTSQNSVYGYGVCSDPANAYSKQCAALAPADKGHYLARKYVVDDEKLQNFSVDTQLQSKFATGDIDHTLLTGVDFMRMRNDINAWFGYDDSVPLLNLYNPVNTDFDFNAKDPANSGPYRILNKQKQTGVYVQDQAQWDKVLVTLGGRYDWADQESLNRVAGTTDKRDDKQFTWRGGVNYLFDNGVTPYFSYSESFEPSSQVGKDGNIFAPSKGKQYEVGVKYVPEDRPIVVTGAVYNLTKTNNLMADPEGSFFSVEGGEIRARGVEIEAKAALSASVNVVGSYTYTDAEYTTDTTYKGNTPAQVPKHMASLWADYTFFDGPLSGLTLGTGGRYTGSSYGDPANSFKVGSYTVVDALVRYDLARVGMAGSNVALHVNNLFDREYVASCFNTYGCFWGAERQVVATATFRF

来源 Source

来源生物 organism	Escherichia coli K-12
NCBI Class编号 ncbi_taxonomy_id	83333
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Lytic conversion lipoprotein
Molecular weight formula_weight	9547.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MKKLFLAMAVVLLSACSTFGPKDIKCEAYYMQDHVKYKANVFDRKGDMFLVSPIMAYGSFWAPVSYFTEGNTCEGVFHHHHHH

来源 Source

来源生物 organism	Escherichia phage T5
NCBI Class编号 ncbi_taxonomy_id	2695836
宿主生物 host_organism	Escherichia coli

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8. Citations (1)

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Unit-cell length a length_a	98.287 Å
Unit-cell length b length_b	98.287 Å
Unit-cell length c length_c	236.588 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	3.370 Å
Low-resolution limit resolution_low	57.850 Å
R factor r_factor	0.2558
R_work r_work	0.2532
R_free r_free	0.3074

fit	/app/data/saxs_computation/a6/8a60/8a60.fit
pddf	/app/data/pr_computation/a6/8a60/8a60.pr.out
profile	/app/data/saxs_computation/a6/8a60/8a60.dat

Crystal structure of FhuA in complex with the superinfection exclusion lipoprotein Llp

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

Ferrichrome outer membrane transporter/phage receptor

State in the Current Structure

Other States of the Same Protein in the Database

Lytic conversion lipoprotein

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)