SAXSdb — 1dkh

▼

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

HEME-BINDING PROTEIN A

Serratia marcescens

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 1–188	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

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 1DKH	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 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 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 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
1YBJ Structural and Dynamics studies of both apo and holo forms of the hemophore HasA Deposited 2004-12-21	Different construct 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 mutation/modification 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
3CSL Structure of the Serratia marcescens hemophore receptor HasR in complex with its hemophore HasA and heme Deposited 2008-04-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 2–188（187 aa）	Not recorded	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
3CSL Structure of the Serratia marcescens hemophore receptor HasR in complex with its hemophore HasA and heme Deposited 2008-04-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 2–188（187 aa）	Not recorded	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
3CSN Structure of the Serratia marcescens hemophore receptor HasR in complex with its hemophore HasA Deposited 2008-04-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions 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 construct Different oligomeric state Different ligand/ion Different experimental conditions 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 construct Different oligomeric state Different ligand/ion Different experimental conditions 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 construct Different oligomeric state Different ligand/ion Different experimental conditions 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 oligomeric state 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 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 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 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 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 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 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 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 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HASA_SERMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–188； UniProt 1–188

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1dkh
Deposition date deposition_date	1999-12-07
Structure title title	CRYSTAL STRUCTURE OF THE HEMOPHORE HASA, PH 6.5
Keywords keywords	TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	16.81 Å
Radius of gyration Rg (electron density) rg_electron	15.47 Å
Forward intensity I(0) i0	7237930.00
Molecular weight molecular_weight	18623.0 kDa
Excluded volume excluded_volume	22628 Å³
Envelope volume envelope_volume	25250 Å³
Hydration-shell volume shell_volume	13962 Å³
Envelope diameter envelope_diameter	52.8 Å
Shell Rg shell_rg	21.10 Å
Envelope Rg envelope_rg	15.65 Å
Shape Rg shape_rg	15.42 Å
Total Rg total_rg	16.52 Å
Total atoms total_atoms	1298
Residues n_residues	172
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

▼

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

Maximum dimension Dmax dmax	52.7 Å
Rg (real space) rg_real	16.70 Å
Rg uncertainty (real space) rg_real_error	0.31 Å
I(0) (real space) i0_real	7.2380e+06
I(0) uncertainty (real space) i0_real_error	8.7890e+04
Rg (reciprocal space) rg_reciprocal	16.72 Å
I(0) (reciprocal space) i0_reciprocal	7238000.0000
Solution quality estimate total_estimate	0.6807
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	21.9 Å
Skewness Skewness skewness	0.108
Kurtosis Kurtosis kurtosis	-0.404
Angular range angular_range	— – 0.4750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	776300.0000
Real-space data points n_real_points	78
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.892; Stabil: 0.999; Sysdev: 0.394; Positv: 1.000; Valcen: 0.989; Smooth: 0.000

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	HEME-BINDING PROTEIN A
Molecular weight formula_weight	19288.6 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	1306

MAFSVNYDSSFGGYSIHDYLGQWASTFGDVNHTNGNVTDANSGGFYGGSLSGSQYAISSTANQVTAFVAGGNLTYTLFNEPAHTLYGQLDSLSFGDGLSGGDTSPYSIQVPDVSFGGLNLSSLQAQGHDGVVHQVVYGLMSGDTGALETALNGILDDYGLSVNSTFDQVAAATAVGVQHADSPELLAA

来源 Source

来源生物 organism	Serratia marcescens
NCBI Class编号 ncbi_taxonomy_id	615
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 3 Entity 3 non-polymer

Description description	SAMARIUM (III) ION
Molecular weight formula_weight	150.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	PROTOPORPHYRIN IX CONTAINING FE
Molecular weight formula_weight	616.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	8

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1dkha_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.35 — Heme-binding protein A (HasA)
Superfamily Superfamily superfamily	d.35.1 — Heme-binding protein A (HasA)
Family Family family	d.35.1.1 — Heme-binding protein A (HasA)

CATH v4.4 (1 domains)

Domain ID domain_id	1dkhA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1500 — Heme-binding Protein A; Chain: A;
Homologous superfamily homologous superfamily	10 — Haem-binding HasA

▶

8. Citations (2)

▶

Unit-cell length a length_a	111.650 Å
Unit-cell length b length_b	111.650 Å
Unit-cell length c length_c	52.790 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	3.200 Å
Low-resolution limit resolution_low	12.000 Å
R factor r_factor	0.2300
R_work r_work	0.2280
R_free r_free	0.2880

fit	/app/data/saxs_computation/dk/1dkh/1dkh.fit
pddf	/app/data/pr_computation/dk/1dkh/1dkh.pr.out
profile	/app/data/saxs_computation/dk/1dkh/1dkh.dat

CRYSTAL STRUCTURE OF THE HEMOPHORE HASA, PH 6.5

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

HEME-BINDING PROTEIN A

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