4cu4

FhuA from E. coli in complex with the lasso peptide microcin J25 (MccJ25)

Method: X-RAY DIFFRACTION D_max: 84.7 Å Quality: GOOD

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

FERRICHROME-IRON RECEPTOR

ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 53–438 Chain A； UniProt 439–747	Fragment：RESIDUES 53-747	MICROCIN J25 × 1 （Q9X2V7） ;L-glycero-alpha-D-manno-heptopyranose-(1-3)-L-glycero-alpha-D-manno-heptopyranose-(1-5)-[3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-4)]3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-6)-2-amino-2-deoxy-beta-D-glucopyranose-(1-6)-2-amino-2-deoxy-alpha-D-glucopyranose ; × 1 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

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 4CU4	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 construct Different mutation/modification 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 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 34–747（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 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 34–747（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 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 34–747（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 mutation/modification 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 mutation/modification 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
8A60 Crystal structure of FhuA in complex with the superinfection exclusion lipoprotein Llp Deposited 2022-06-16	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 A 34–747（714 aa）	Not recorded	No recorded non-water small molecule	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
8A8C T5 phage receptor-binding protein pb5 bound to ferrichrome transporter FhuA Deposited 2022-06-22	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 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 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 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 1–386； UniProt 53–438 Author chain A； PDBConstruct 398–706； UniProt 439–747

MICROCIN J25

OrganismNot specified

UniProt Q9X2V7

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 38–58	Not recorded	FERRICHROME-IRON RECEPTOR × 1 （P06971） ;L-glycero-alpha-D-manno-heptopyranose-(1-3)-L-glycero-alpha-D-manno-heptopyranose-(1-5)-[3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-4)]3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-6)-2-amino-2-deoxy-beta-D-glucopyranose-(1-6)-2-amino-2-deoxy-alpha-D-glucopyranose ; × 1 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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 4CU4	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1PP5 Structure of Antibacterial Peptide Microcin J25: a 21-Residue Lariat Protoknot Deposited 2003-06-16	Different oligomeric state 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 38–58（21 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions 298 K；Ionic strength (raw mmCIF value) NA；Pressure ambient NMR sample composition 2mM Microcin J25 U-13C,15N; 99.5% CD3OH, 0.5% H2O \| 99.5% CD3OH, 0.5% H2O	Resolution not provided
1Q71 The structure of microcin J25 is a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone Deposited 2003-08-14	Different oligomeric state 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 38–58（21 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions 298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 0.3 mg of microcin J25 \| 100% CD3OH	Resolution not provided
1S7P Solution structure of thermolysin digested microcin J25 Deposited 2004-01-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 38–47（10 aa） Fragment：Residues 38-47 Chain B 48–58（11 aa） Fragment：Residues 48-58	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions 295 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 6mM t-MccJ25 \| 100% CD3OH	Resolution not provided
2MMT Lasso peptide-based integrin inhibitor: Microcin J25 variant with RGDF substitution of Gly12-Ile13-Gly14-Thr15 Deposited 2014-03-18	Different construct Different mutation/modification Different oligomeric state 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 38–58（21 aa） Fragment：UNP residues 38-58	Mutation：G12R/I13G/G14D/T15F	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions 298 K；Pressure 1.0 NMR sample composition 12.6 mM MCCJ25(RGDF), methanol \| methanol	Resolution not provided
2MMW LASSO PEPTIDE BASED INTEGRIN INHIBITOR: MICROCIN J25 VARIANT WITH RGD SUBSTITUTION of GLY12-ILE13-GLY14 Deposited 2014-03-20	Different mutation/modification Different oligomeric state 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 38–58（21 aa）	Mutation：G12R, I13G, G14D	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions 298 K；Pressure ambient NMR sample composition 11.6 mM MCCJ25(RGD), methanol \| methanol	Resolution not provided
5T56 [3]catenane from MccJ25 G12R/I13C/G21C lasso peptide Deposited 2016-08-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 38–48（11 aa） Chain B 51–57（7 aa） Chain C 38–48（11 aa） Chain D 51–57（7 aa）	Mutation：UNP residues 38-48 Mutation：UNP residues 51-57 Mutation：UNP residues 38-48 Mutation：UNP residues 51-57	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions 295 K；Pressure ambient NMR sample composition 3.7 mg/mL [3]catenane from MccJ25 RCC lasso peptide, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
6N60 Escherichia coli RNA polymerase sigma70-holoenzyme bound to upstream fork promoter DNA and Microcin J25 (MccJ25) Deposited 2018-11-23	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 7 PDB declaration: nonameric	Chain M 38–58（21 aa） Fragment：UNP residues 38-58	Not recorded	MG MAGNESIUM ION × 1 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；295 K；0.1 M HEPES, pH 6.7, 0.2 M magnesium chloride, 7% w/v PEG3350, 4% v/v glycerol	Resolution 3.68 Å R-free 0.306

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MCJA_ECOLX
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–21； UniProt 38–58

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	4cu4
Deposition date deposition_date	2014-03-17
Structure title title	FhuA from E. coli in complex with the lasso peptide microcin J25 (MccJ25)
Keywords keywords	TRANSPORT PROTEIN-ANTIBIOTIC COMPLEX, LIPOPOLYSACCHARIDE, DETERGENT; TRANSPORT PROTEIN/ANTIBIOTIC
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	26.65 Å
Radius of gyration Rg (electron density) rg_electron	26.17 Å
Forward intensity I(0) i0	110693000.00
Molecular weight molecular_weight	86164.0 kDa
Excluded volume excluded_volume	109220 Å³
Envelope volume envelope_volume	130970 Å³
Hydration-shell volume shell_volume	39792 Å³
Envelope diameter envelope_diameter	88.8 Å
Shell Rg shell_rg	35.29 Å
Envelope Rg envelope_rg	26.35 Å
Shape Rg shape_rg	26.15 Å
Total Rg total_rg	27.18 Å
Total atoms total_atoms	6074
Residues n_residues	714
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	84.7 Å
Rg (real space) rg_real	26.51 Å
Rg uncertainty (real space) rg_real_error	0.48 Å
I(0) (real space) i0_real	1.1070e+08
I(0) uncertainty (real space) i0_real_error	1.5380e+06
Rg (reciprocal space) rg_reciprocal	26.56 Å
I(0) (reciprocal space) i0_reciprocal	110700000.0000
Solution quality estimate total_estimate	0.8887
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	33.9 Å
Skewness Skewness skewness	0.230
Kurtosis Kurtosis kurtosis	-0.275
Angular range angular_range	— – 0.3000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	23040000.0000
Real-space data points n_real_points	61
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.995

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (11)

Entity 1 Entity 1 polymer

Description description	FERRICHROME-IRON RECEPTOR
Molecular weight formula_weight	78101.0 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	6260

SAWGPAATIAARQSATGTKTDTPIQKVPQSISVVTAEEMALHQPKSVKEALSYTPGVSVGTRGASNTYDHLIIRGFAAEGQSQNNYLNGLKLQGNFYNDAVIDPYMLERAEIMRGPVSVLYGKSSPGGLLNMVSKRPTTEPLKEVQFKAGTDSLFQTGFDFSDSLDDDGVYSYRLTGLARSANAQQKGSEEQRYAIAPAFTWRPDDKTNFTFLSYFQNEPETGYYGWLPKEGTVEPLPNGKRLPTDFNEGAKNNTYSRNEKMVGYSFDHEFNDTFTVRQNLRFAENKTSQNSVYGYGVCSDPANAYSKQCAALAPADKGHYLARKYVVDDEKLQNFSVDTQLQSKFATGDIDHTLLTGVDFMRMRNDINAWFGYDDSVPLLNLYNPSSHHHHHHGSSVNTDFDFNAKDPANSGPYRILNKQKQTGVYVQDQAQWDKVLVTLGGRYDWADQESLNRVAGTTDKRDDKQFTWRGGVNYLFDNGVTPYFSYSESFEPSSQVGKDGNIFAPSKGKQYEVGVKYVPEDRPIVVTGAVYNLTKTNNLMADPEGSFFSVEGGEIRARGVEIEAKAALSASVNVVGSYTYTDAEYTTDTTYKGNTPAQVPKHMASLWADYTFFDGPLSGLTLGTGGRYTGSSYGDPANSFKVGSYTVVDALVRYDLARVGMAGSNVALHVNNLFDREYVASCFNTYGCFWGAERQVVATATFRF

来源 Source

来源生物 organism	ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655
NCBI Class编号 ncbi_taxonomy_id	511145
宿主生物 host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	MICROCIN J25
Molecular weight formula_weight	2126.3 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

GGAGHVPEYFVGIGTPISFYG

Entity 3 Entity 3 branched

Description description	;L-glycero-alpha-D-manno-heptopyranose-(1-3)-L-glycero-alpha-D-manno-heptopyranose-(1-5)-[3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-4)]3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-6)-2-amino-2-deoxy-beta-D-glucopyranose-(1-6)-2-amino-2-deoxy-alpha-D-glucopyranose ;
Molecular weight formula_weight	1165.0 kDa
Source method src_method	man
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	3-HYDROXY-TETRADECANOIC ACID
Molecular weight formula_weight	244.4 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 5 Entity 5 non-polymer

Description description	LAURIC ACID
Molecular weight formula_weight	200.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 non-polymer

Description description	MYRISTIC ACID
Molecular weight formula_weight	228.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 7 Entity 7 non-polymer

Description description	LAURYL DIMETHYLAMINE-N-OXIDE
Molecular weight formula_weight	229.4 kDa
Source method src_method	syn
Copy count entity_count	20

Entity 8 Entity 8 non-polymer

Description description	1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE
Molecular weight formula_weight	705.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 9 Entity 9 non-polymer

Description description	DIPHOSPHATE
Molecular weight formula_weight	173.9 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 10 Entity 10 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 11 Entity 11 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	168

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d4cu4a_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.4 — Transmembrane beta-barrels
Superfamily Superfamily superfamily	f.4.3 — Porins
Family Family family	f.4.3.3 — Ligand-gated protein channel

Domain ID domain_id	d4cu4b_
Class class	j — Peptides
Fold Fold fold	j.5 — Macrocyclic bacteriocins
Superfamily Superfamily superfamily	j.5.1 — Macrocyclic bacteriocins
Family Family family	j.5.1.1 — Microcin J25

CATH v4.4 (2 domains)

Domain ID domain_id	4cu4A01
Class class	2 — Mainly Beta
Architecture architecture	170 — Beta Complex
Topology topology	130 — Ferric Hydroxamate Uptake Protein; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — TonB-dependent receptor, plug domain

Domain ID domain_id	4cu4A02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	170 — Maltoporin; Chain A
Homologous superfamily homologous superfamily	20 — TonB-dependent receptor, beta-barrel domain

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8. Citations (1)

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Unit-cell length a length_a	95.980 Å
Unit-cell length b length_b	277.050 Å
Unit-cell length c length_c	106.760 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	2.300 Å
Low-resolution limit resolution_low	30.460 Å
R factor r_factor	0.2141
R_work r_work	0.2120
R_free r_free	0.2550

fit	/app/data/saxs_computation/cu/4cu4/4cu4.fit
pddf	/app/data/pr_computation/cu/4cu4/4cu4.pr.out
profile	/app/data/saxs_computation/cu/4cu4/4cu4.dat

FhuA from E. coli in complex with the lasso peptide microcin J25 (MccJ25)

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

FERRICHROME-IRON RECEPTOR

State in the Current Structure

Other States of the Same Protein in the Database

MICROCIN J25

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 (11)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 branched

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 non-polymer

Entity 11 Entity 11 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)