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3csl

Structure of the Serratia marcescens hemophore receptor HasR in complex with its hemophore HasA and heme

Method: X-RAY DIFFRACTION Dmax: 178.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

HasR protein

Serratia marcescens

UniProt Q79AD2

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 35–899 Not recorded Hemophore HasA × 1 （Q54450） HEM PROTOPORPHYRIN IX CONTAINING FE × 1 GOL GLYCEROL × 5 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；2 M NaCl, 100 mM Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.70 Å R-free 0.274
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain B； UniProt 35–899 Not recorded Hemophore HasA × 1 （Q54450） HEM PROTOPORPHYRIN IX CONTAINING FE × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；2 M NaCl, 100 mM Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.70 Å R-free 0.274

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 3CSL Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2M5J Solution structure of the periplasmic signaling domain of HasR, a TonB-dependent outer membrane heme transporter Deposited 2013-02-26 Different construct 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 42–146（105 aa） Fragment：UNP residues 42-146
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；293 K；Ionic strength (raw mmCIF value) 0.1；Pressure 1
NMR sample composition 0.5 mM [U-99% 13C; U-99% 15N] HasR_N-terminal_periplasmic_signaling_domain-1, 50 mM Sodium phosphate-2, 50 mM NaCl-3, 85% H2O/15% D2O | 85% H2O/15% D2O
Resolution not provided
3CSN Structure of the Serratia marcescens hemophore receptor HasR in complex with its hemophore HasA Deposited 2008-04-10 Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 35–899（865 aa）
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；291 K；2 M NaCl, 100 mM Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 3.00 Å R-free 0.244
3CSN Structure of the Serratia marcescens hemophore receptor HasR in complex with its hemophore HasA Deposited 2008-04-10 Different ligand/ion Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 35–899（865 aa）
Not recorded GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；291 K；2 M NaCl, 100 mM Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 3.00 Å R-free 0.244
3DDR Structure of the Serratia marcescens hemophore receptor HasR-Ile671Gly mutant in complex with its hemophore HasA and heme Deposited 2008-06-06 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 48–899（852 aa） Fragment：UNP residues 48 to 899
Mutation：I671G NA SODIUM ION × 1 GOL GLYCEROL × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；291 K；2 M NaCl, 100 mM Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.80 Å R-free 0.262
3DDR Structure of the Serratia marcescens hemophore receptor HasR-Ile671Gly mutant in complex with its hemophore HasA and heme Deposited 2008-06-06 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 48–899（852 aa） Fragment：UNP residues 48 to 899
Mutation：I671G NA SODIUM ION × 1 GOL GLYCEROL × 5 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；291 K；2 M NaCl, 100 mM Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.80 Å R-free 0.262
5C58 A double mutant of serratia marcescens hemophore receptor HasR in complex with its hemophore HasA and heme Deposited 2015-06-19 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 35–899（865 aa）
Mutation：R297A, N800A HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；100mM Tris pH 7 to 8, 1.8 to 2.2mM NaCl, 100mM K2HPO4
Resolution 2.79 Å R-free 0.296

4 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q79AD2_SERMA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–865； UniProt 35–899 Author chain B； PDBConstruct 1–865； UniProt 35–899

Hemophore HasA

Serratia marcescens

UniProt Q54450

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 C； UniProt 2–188 Not recorded HasR protein × 1 （Q79AD2） HEM PROTOPORPHYRIN IX CONTAINING FE × 1 GOL GLYCEROL × 5 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；2 M NaCl, 100 mM Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.70 Å R-free 0.274
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain D； UniProt 2–188 Not recorded HasR protein × 1 （Q79AD2） HEM PROTOPORPHYRIN IX CONTAINING FE × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；2 M NaCl, 100 mM Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.70 Å R-free 0.274

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 3CSL Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1B2V HEME-BINDING PROTEIN A Deposited 1998-12-01 Different construct 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 1–188（188 aa）
Not recorded CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.6；0.2M CACL, 0.1M NA ACETATE PH 4.6, 20% ISOPRPANOL
Resolution 1.90 Å R-free 0.218
1DK0 CRYSTAL STRUCTURE OF THE HEMOPHORE HASA FROM SERRATIA MARCESCENS CRYSTAL FORM P2(1), PH8 Deposited 1999-12-06 Different construct 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 1–188（188 aa）
Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M NaHepes, pH8.0, 1.4M NaKTartrate, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.77 Å R-free 0.213
1DK0 CRYSTAL STRUCTURE OF THE HEMOPHORE HASA FROM SERRATIA MARCESCENS CRYSTAL FORM P2(1), PH8 Deposited 1999-12-06 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–188（188 aa）
Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M NaHepes, pH8.0, 1.4M NaKTartrate, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.77 Å R-free 0.213
1DKH CRYSTAL STRUCTURE OF THE HEMOPHORE HASA, PH 6.5 Deposited 1999-12-07 Different construct 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 1–188（188 aa）
Not recorded ZN ZINC ION × 3 SM SAMARIUM (III) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；Cacodylate buffer pH6.5, Zinc Acetate 140mM, Glycerol 2%, PEG8000 10%, Samarium Chloride 10mM., VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.20 Å R-free 0.288
1YBJ Structural and Dynamics studies of both apo and holo forms of the hemophore HasA Deposited 2004-12-21 Different construct 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 2–179（178 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.6；303 K；Ionic strength (raw mmCIF value) 20mM sodium phosphate buffer；Pressure ambient
NMR sample composition 1.8mM HasA 15N | 20mM sodium phosphate buffer, pH5.6; 90% H2O/10% D20
NMR sample composition 1.9mM HasA 15N,13C | 20mM sodium phosphate buffer, pH5.6; 90% H2O/10% D20
Resolution not provided
2CN4 The crystal structure of the secreted dimeric form of the hemophore HasA reveals a domain swapping with an exchanged heme ligand Deposited 2006-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–174（173 aa）
Chain B 2–174（173 aa）
Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 2 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；2 MICROLITERS PROTEIN (AT A CONCENTRATION OF ABOUT 4 MG/ML) WERE MIXED WITH 1 MICROLITER RESERVOIR CONSISTING OF 100 MM TRIS BUFFER AT PH 8.5, 2 M K2HPO4 AND 2 M NAH2PO4.
Resolution 2.30 Å R-free 0.224
2UYD Crystal structure of the SmHasA mutant H83A Deposited 2007-04-04 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 X 1–188（188 aa）
Mutation：YES HEM PROTOPORPHYRIN IX CONTAINING FE × 1 ZN ZINC ION × 8 ACT ACETATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；293 K；DROPS WERE PREPARED BY MIXING 2MICROL OF THE PROTEIN SOLUTION WITH 1 MICROL OF THE RESERVOIR SOLUTION THAT CONTAINED 100 MM SODIUM CACODYLATE AT PH 6.5, 200 MM ZN(OAC)2 AND 10 % (V/V) 2-PROPANOL. THE BROWNISH CRYSTALS GREW OVER A PERIOD OF 2 MONTHS AT 20 DEGREES C.
Resolution 2.70 Å R-free 0.274
3CSN Structure of the Serratia marcescens hemophore receptor HasR in complex with its hemophore HasA Deposited 2008-04-10 Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 2–188（187 aa）
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；291 K；2 M NaCl, 100 mM Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 3.00 Å R-free 0.244
3CSN Structure of the Serratia marcescens hemophore receptor HasR in complex with its hemophore HasA Deposited 2008-04-10 Different ligand/ion Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 2–188（187 aa）
Not recorded GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；291 K；2 M NaCl, 100 mM Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 3.00 Å R-free 0.244
3DDR Structure of the Serratia marcescens hemophore receptor HasR-Ile671Gly mutant in complex with its hemophore HasA and heme Deposited 2008-06-06 Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 2–188（187 aa）
Not recorded NA SODIUM ION × 1 GOL GLYCEROL × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；291 K；2 M NaCl, 100 mM Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.80 Å R-free 0.262
3DDR Structure of the Serratia marcescens hemophore receptor HasR-Ile671Gly mutant in complex with its hemophore HasA and heme Deposited 2008-06-06 Different ligand/ion Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 2–188（187 aa）
Not recorded NA SODIUM ION × 1 GOL GLYCEROL × 5 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；291 K；2 M NaCl, 100 mM Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.80 Å R-free 0.262
5C58 A double mutant of serratia marcescens hemophore receptor HasR in complex with its hemophore HasA and heme Deposited 2015-06-19 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 2–188（187 aa） Fragment：UNP residues 2-188
Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；100mM Tris pH 7 to 8, 1.8 to 2.2mM NaCl, 100mM K2HPO4
Resolution 2.79 Å R-free 0.296
9XOH Crystal Structure of Redesigned HasAsm Variant (14-mutation) with Iron Tetraphenylporphyrin Deposited 2025-11-13 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 1–176（176 aa）
Mutation：A2S, G13A, H17A, G21T, S42T, Q63N, N79S, D102T, V110N, D112E, A125S, V131E, G145S, D156K MQP [5,10,15,20-tetraphenylporphyrinato(2-)-kappa~4~N~21~,N~22~,N~23~,N~24~]iron × 1 GOL GLYCEROL × 3 NA SODIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1M sodium cacodylate-HCl, 1M sodium citrate tribasic
Resolution 1.51 Å R-free 0.234
9XOH Crystal Structure of Redesigned HasAsm Variant (14-mutation) with Iron Tetraphenylporphyrin Deposited 2025-11-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–176（176 aa）
Mutation：A2S, G13A, H17A, G21T, S42T, Q63N, N79S, D102T, V110N, D112E, A125S, V131E, G145S, D156K MQP [5,10,15,20-tetraphenylporphyrinato(2-)-kappa~4~N~21~,N~22~,N~23~,N~24~]iron × 1 GOL GLYCEROL × 2 NA SODIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1M sodium cacodylate-HCl, 1M sodium citrate tribasic
Resolution 1.51 Å R-free 0.234
9XOH Crystal Structure of Redesigned HasAsm Variant (14-mutation) with Iron Tetraphenylporphyrin Deposited 2025-11-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 1–176（176 aa）
Mutation：A2S, G13A, H17A, G21T, S42T, Q63N, N79S, D102T, V110N, D112E, A125S, V131E, G145S, D156K MQP [5,10,15,20-tetraphenylporphyrinato(2-)-kappa~4~N~21~,N~22~,N~23~,N~24~]iron × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1M sodium cacodylate-HCl, 1M sodium citrate tribasic
Resolution 1.51 Å R-free 0.234
9XOH Crystal Structure of Redesigned HasAsm Variant (14-mutation) with Iron Tetraphenylporphyrin Deposited 2025-11-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 1–176（176 aa）
Mutation：A2S, G13A, H17A, G21T, S42T, Q63N, N79S, D102T, V110N, D112E, A125S, V131E, G145S, D156K MQP [5,10,15,20-tetraphenylporphyrinato(2-)-kappa~4~N~21~,N~22~,N~23~,N~24~]iron × 1 GOL GLYCEROL × 2 NA SODIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1M sodium cacodylate-HCl, 1M sodium citrate tribasic
Resolution 1.51 Å R-free 0.234
9XOK Crystal Structure of Redesigned HasAsm Variant (51-mutation) with Iron Tetraphenylporphyrin Deposited 2025-11-13 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 3–173（171 aa）
Mutation：;F11L, G12D, G13N, Y14L, S15T, I16L, H17Q, D18E, Y19F, L20F, G21N, Q22E, S25A, T26S, S58T, A61K, N62D, Q63G, Q88T, S93A, D96N, D102S, T103S, S104T, Q109T, V110E, D112Q, V113F, S114R, F115L, N119G, L120W, S121T, L123E, Q124I, A125S, Q126E, T144S, G145T, A146P, E148L, T149Q, G153N, I154Q, D156Q, D157Q, V162T, D167M, Q168E, V169I, A170R ; MQP [5,10,15,20-tetraphenylporphyrinato(2-)-kappa~4~N~21~,N~22~,N~23~,N~24~]iron × 1 SO4 SULFATE ION × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1M sodium cacodylate-HCl, 2M ammonium sulfate, 0.2M NaCl
Resolution 1.80 Å R-free 0.330
9XPD Crystal Structure of Redesigned HasAsm Variant (51-mutation) with Heme Deposited 2025-11-16 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 1–176（176 aa）
Mutation：;F11L, G12D, G13N, Y14L, S15T, I16L, H17Q, D18E, Y19F, L20F, G21N, Q22E, S25A, T26S, S58T, A61K, N62D, Q63G, Q88T, S93A, D96N, D102S, T103S, S104T, Q109T, V110E, D112Q, V113F, S114R, F115L, N119G, L120W, S121T, L123E, Q124I, A125S, Q126E, T144S, G145T, A146P, E148L, T149Q, G153N, I154Q, D156Q, D157Q, V162T, D167M, Q168E, V169I, A170R ; IMD IMIDAZOLE × 1 CIT CITRIC ACID × 1 GOL GLYCEROL × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；0.1M imidazole-HCl, 1M sodium citrate tribasic
Resolution 1.22 Å R-free 0.177
9XPI Crystal Structure of Redesigned HasAsm Variant (48-mutation) with Heme Deposited 2025-11-16 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 1–176（176 aa）
Mutation：;F11L, G12A, G13N, Y14L, S15T, I16L, H17A, D18E, Y19F, L20F, G21N, Q22E, T26Y, N41S, S58T, A61K, N62D, Q63G, N79S, E80P, Q88T, S91A, S93T, D96N, T103S, S104T, Q109V, V110N, D112E, S114T, G116S, L120W, S121T, L123E, A125E, Q126E, Q134K, V136I, G145T, E148L, T149Q, G153S, I154L, D156K, D157Q, V162I, Q168E, V169I ; HEM PROTOPORPHYRIN IX CONTAINING FE × 1 ACT ACETATE ION × 3 ZN ZINC ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；0.1M imidazole-HCl, 2.5M NaCl, 0.2M Zinc acetate
Resolution 2.16 Å R-free 0.255

13 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HASA_SERMA
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C； PDBConstruct 20–206； UniProt 2–188 Author chain D； PDBConstruct 20–206； UniProt 2–188

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

SAXS profile for 3csl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3csl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3csl
Deposition date deposition_date2008-04-10
Structure title titleStructure of the Serratia marcescens hemophore receptor HasR in complex with its hemophore HasA and heme
Keywords keywords;outer membrane protein, beta-barrel, hemophore receptor, TonB box, Heme, Iron, Metal-binding, Secreted, MEMBRANE PROTEIN-HEME BINDING PROTEIN COMPLEX ;; MEMBRANE PROTEIN/HEME BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier52.51 Å
Radius of gyration Rg (electron density) rg_electron52.79 Å
Forward intensity I(0) i0631833000.00
Molecular weight molecular_weight201980.0 kDa
Excluded volume excluded_volume249160 ų
Envelope volume envelope_volume344660 ų
Hydration-shell volume shell_volume56226 ų
Envelope diameter envelope_diameter188.4 Å
Shell Rg shell_rg53.36 Å
Envelope Rg envelope_rg52.03 Å
Shape Rg shape_rg52.79 Å
Total Rg total_rg52.81 Å
Total atoms total_atoms14274
Residues n_residues1832
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax178.5 Å
Rg (real space) rg_real52.96 Å
Rg uncertainty (real space) rg_real_error2.55 Å
I(0) (real space) i0_real6.3180e+08
I(0) uncertainty (real space) i0_real_error1.2420e+07
Rg (reciprocal space) rg_reciprocal52.12 Å
I(0) (reciprocal space) i0_reciprocal631100000.0000
Solution quality estimate total_estimate0.7541
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary35.7 Å
Skewness Skewness skewness0.466
Kurtosis Kurtosis kurtosis-0.517
Angular range angular_range— – 0.1500 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha125000000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.511; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.737; Smooth: 0.537
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3cslc1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.35 — Heme-binding protein A (HasA)
Superfamily Superfamily superfamilyd.35.1 — Heme-binding protein A (HasA)
Family Family familyd.35.1.1 — Heme-binding protein A (HasA)
Domain ID domain_idd3cslc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3csld1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.35 — Heme-binding protein A (HasA)
Superfamily Superfamily superfamilyd.35.1 — Heme-binding protein A (HasA)
Family Family familyd.35.1.1 — Heme-binding protein A (HasA)
Domain ID domain_idd3csld2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (6 domains)

Domain ID domain_id3cslA01
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology130 — Ferric Hydroxamate Uptake Protein; Chain A, domain 1
Homologous superfamily homologous superfamily10 — TonB-dependent receptor, plug domain
Domain ID domain_id3cslA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology170 — Maltoporin; Chain A
Homologous superfamily homologous superfamily20 — TonB-dependent receptor, beta-barrel domain
Domain ID domain_id3cslB01
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology130 — Ferric Hydroxamate Uptake Protein; Chain A, domain 1
Homologous superfamily homologous superfamily10 — TonB-dependent receptor, plug domain
Domain ID domain_id3cslB02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology170 — Maltoporin; Chain A
Homologous superfamily homologous superfamily20 — TonB-dependent receptor, beta-barrel domain
Domain ID domain_id3cslC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1500 — Heme-binding Protein A; Chain: A;
Homologous superfamily homologous superfamily10 — Haem-binding HasA
Domain ID domain_id3cslD00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1500 — Heme-binding Protein A; Chain: A;
Homologous superfamily homologous superfamily10 — Haem-binding HasA
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8. Citations (1)

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9. Files and Curves (10)