3zow

Crystal Structure of Wild Type Nitrosomonas europaea Cytochrome c552

Method: X-RAY DIFFRACTION D_max: 134.0 Å Quality: GOOD

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

CYTOCHROME C-552

OrganismNot specified

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 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
10	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain J； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
11	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain K； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
12	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain L； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
13	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain M； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
14	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain N； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
15	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain O； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
16	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain P； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
17	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain Q； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
18	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain R； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
3	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain C； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
4	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain D； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
5	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain E； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
6	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain F； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
7	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain G； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
8	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain H； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258
9	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain I； UniProt 23–103	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；3 M AMMONIUM SULFATE, 10 MM TRIS-HCL PH 8	Resolution 2.35 Å R-free 0.258

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 3ZOW	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A56 PRIMARY SEQUENCE AND SOLUTION CONFORMATION OF FERRICYTOCHROME C-552 FROM NITROSOMONAS EUROPAEA, NMR, MEAN STRUCTURE REFINED WITH EXPLICIT HYDROGEN BOND CONSTRAINTS Deposited 1998-02-20	Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 23–103（81 aa）	Not recorded	HEC HEME C × 1	SOLUTION NMR NMR measurement conditions pH 6.9；323 K；Ionic strength (raw mmCIF value) 0.05；Pressure 1 NMR sample composition WATER	Resolution not provided
1A8C PRIMARY SEQUENCE AND SOLUTION CONFORMATION OF FERROCYTOCHROME C-552 FROM NITROSOMONAS EUROPAEA, NMR, MEAN STRUCTURE REFINED WITHOUT HYDROGEN BOND CONSTRAINTS Deposited 1998-03-23	Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 23–103（81 aa）	Not recorded	HEC HEME C × 1	SOLUTION NMR NMR measurement conditions pH 6.9；323 K；Ionic strength (raw mmCIF value) 0.05；Pressure 1 NMR sample composition WATER	Resolution not provided
3ZOX Crystal Structure of N64Del Mutant of Nitrosomonas europaea Cytochrome c552 (monoclinic space group) Deposited 2013-02-26	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 23–103（81 aa）	Mutation：YES	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 9.5；0.1 M CHES PH 9.5, 30% (W/V) PEG 8000	Resolution 2.10 Å R-free 0.274
3ZOX Crystal Structure of N64Del Mutant of Nitrosomonas europaea Cytochrome c552 (monoclinic space group) Deposited 2013-02-26	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 23–103（81 aa）	Mutation：YES	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 9.5；0.1 M CHES PH 9.5, 30% (W/V) PEG 8000	Resolution 2.10 Å R-free 0.274
3ZOX Crystal Structure of N64Del Mutant of Nitrosomonas europaea Cytochrome c552 (monoclinic space group) Deposited 2013-02-26	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 23–103（81 aa）	Mutation：YES	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 9.5；0.1 M CHES PH 9.5, 30% (W/V) PEG 8000	Resolution 2.10 Å R-free 0.274
3ZOX Crystal Structure of N64Del Mutant of Nitrosomonas europaea Cytochrome c552 (monoclinic space group) Deposited 2013-02-26	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 23–103（81 aa）	Mutation：YES	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 9.5；0.1 M CHES PH 9.5, 30% (W/V) PEG 8000	Resolution 2.10 Å R-free 0.274
3ZOY Crystal Structure of N64Del Mutant of Nitrosomonas europaea Cytochrome c552 (hexagonal space group) Deposited 2013-02-26	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 23–103（81 aa）	Mutation：YES	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；0.1 M TRIS-HCL PH 8.5, 3.1 M AMMONIUM SULFATE	Resolution 2.30 Å R-free 0.226
3ZOY Crystal Structure of N64Del Mutant of Nitrosomonas europaea Cytochrome c552 (hexagonal space group) Deposited 2013-02-26	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 23–103（81 aa）	Mutation：YES	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；0.1 M TRIS-HCL PH 8.5, 3.1 M AMMONIUM SULFATE	Resolution 2.30 Å R-free 0.226
3ZOY Crystal Structure of N64Del Mutant of Nitrosomonas europaea Cytochrome c552 (hexagonal space group) Deposited 2013-02-26	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 23–103（81 aa）	Mutation：YES	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；0.1 M TRIS-HCL PH 8.5, 3.1 M AMMONIUM SULFATE	Resolution 2.30 Å R-free 0.226
3ZOY Crystal Structure of N64Del Mutant of Nitrosomonas europaea Cytochrome c552 (hexagonal space group) Deposited 2013-02-26	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 23–103（81 aa）	Mutation：YES	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；0.1 M TRIS-HCL PH 8.5, 3.1 M AMMONIUM SULFATE	Resolution 2.30 Å R-free 0.226
4JCG Recombinant wild type Nitrosomonas europaea cytochrome c552 Deposited 2013-02-21	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 23–103（81 aa） Fragment：Cyt C552 (UNP Residues 23-103)	Not recorded	HEC HEME C × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；277 K；19% (w/v) PEG 6000, 0.2 M LiCl, 0.1 M Tris-HCl pH 7.4 at 7-8 mM protein concentration., VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.63 Å R-free 0.234

5 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CY552_NITEU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–81； UniProt 23–103 Author chain B； PDBConstruct 1–81； UniProt 23–103 Author chain C； PDBConstruct 1–81； UniProt 23–103 Author chain D； PDBConstruct 1–81； UniProt 23–103 Author chain E； PDBConstruct 1–81； UniProt 23–103 Author chain F； PDBConstruct 1–81； UniProt 23–103 Author chain G； PDBConstruct 1–81； UniProt 23–103 Author chain H； PDBConstruct 1–81； UniProt 23–103 Author chain I； PDBConstruct 1–81； UniProt 23–103 Author chain J； PDBConstruct 1–81； UniProt 23–103 Author chain K； PDBConstruct 1–81； UniProt 23–103 Author chain L； PDBConstruct 1–81； UniProt 23–103 Author chain M； PDBConstruct 1–81； UniProt 23–103 Author chain N； PDBConstruct 1–81； UniProt 23–103 Author chain O； PDBConstruct 1–81； UniProt 23–103 Author chain P； PDBConstruct 1–81； UniProt 23–103 Author chain Q； PDBConstruct 1–81； UniProt 23–103 Author chain R； PDBConstruct 1–81； UniProt 23–103

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	3zow
Deposition date deposition_date	2013-02-25
Structure title title	Crystal Structure of Wild Type Nitrosomonas europaea Cytochrome c552
Keywords keywords	HEMEPROTEIN, ELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	41.92 Å
Radius of gyration Rg (electron density) rg_electron	41.63 Å
Forward intensity I(0) i0	376328000.00
Molecular weight molecular_weight	162780.0 kDa
Excluded volume excluded_volume	205370 Å³
Envelope volume envelope_volume	293520 Å³
Hydration-shell volume shell_volume	59418 Å³
Envelope diameter envelope_diameter	139.9 Å
Shell Rg shell_rg	46.63 Å
Envelope Rg envelope_rg	40.36 Å
Shape Rg shape_rg	41.61 Å
Total Rg total_rg	41.99 Å
Total atoms total_atoms	11414
Residues n_residues	1449
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	134.0 Å
Rg (real space) rg_real	41.89 Å
Rg uncertainty (real space) rg_real_error	1.30 Å
I(0) (real space) i0_real	3.7630e+08
I(0) uncertainty (real space) i0_real_error	6.2640e+06
Rg (reciprocal space) rg_reciprocal	41.92 Å
I(0) (reciprocal space) i0_reciprocal	376300000.0000
Solution quality estimate total_estimate	0.8882
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	45.8 Å
Skewness Skewness skewness	0.277
Kurtosis Kurtosis kurtosis	-0.527
Angular range angular_range	— – 0.1900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	26670000.0000
Real-space data points n_real_points	39
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.924; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.772

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (18 domains)

Domain ID domain_id	d3zowa_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowb_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowc_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowd_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowe_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowf_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowg_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowh_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowi_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowj_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowk_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowl_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowm_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zown_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowo_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowp_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowq_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

Domain ID domain_id	d3zowr_
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.1 — monodomain cytochrome c

CATH v4.4 (18 domains)

Domain ID domain_id	3zowA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowC00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowD00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowE00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowF00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowG00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowH00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowI00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowJ00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowK00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowL00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowM00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowN00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowO00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowP00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowQ00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	3zowR00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

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8. Citations (1)

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Unit-cell length a length_a	59.450 Å
Unit-cell length b length_b	137.930 Å
Unit-cell length c length_c	204.660 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	72

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.350 Å
Low-resolution limit resolution_low	35.220 Å
R factor r_factor	0.2041
R_work r_work	0.2011
R_free r_free	0.2576

Description description	CYTOCHROME C-552
Molecular weight formula_weight	8491.7 kDa
EC 编号 ec_number	1.7.2.2
Source method src_method	nat
Copy count entity_count	18

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R
Atom count atom_count	11630

Crystal Structure of Wild Type Nitrosomonas europaea Cytochrome c552

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

CYTOCHROME C-552

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (18 domains)

CATH v4.4 (18 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	HEME C
Molecular weight formula_weight	618.5 kDa
Source method src_method	syn
Copy count entity_count	18

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	216

fit	/app/data/saxs_computation/zo/3zow/3zow.fit
pddf	/app/data/pr_computation/zo/3zow/3zow.pr.out
profile	/app/data/saxs_computation/zo/3zow/3zow.dat