SAXSdb — 2cj1

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

CHLOROPEROXIDASE

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	Other combination Monomer Protein × 1 其他Polymer 2 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 21–319	Fragment：RESIDUES 21-319 Non-standard monomer：Yes (specific site not provided by mmCIF)	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose × 1 MN MANGANESE (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MAN alpha-D-mannopyranose × 12 EDO 1,2-ETHANEDIOL × 3 FMT FORMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 3.6；100 MM SODIUM FORMATE, 24 % PEG 3000, 0.1 M CITRATE PH 3.6 CRYOPROTECTANT CONTAINED 15 % ETHYLENE GLYCOL	Resolution 1.70 Å R-free 0.229

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 2CJ1	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CPO CHLOROPEROXIDASE Deposited 1996-02-10	Different construct 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 22–319（298 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MAN alpha-D-mannopyranose × 9 XYS alpha-D-xylopyranose × 1 MN MANGANESE (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.90 Å R-free 0.224
2CIV Chloroperoxidase bromide complex Deposited 2006-03-26	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 21–319（299 aa） Fragment：RESIDUES 21-319	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MAN alpha-D-mannopyranose × 10 BR BROMIDE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions pH 3.6；22 % PEG3000, 0.1 M KBR, 0.1 M CITRATE PH 3.6	Resolution 1.80 Å R-free 0.184
2CIW Chloroperoxidase iodide complex Deposited 2006-03-26	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 21–319（299 aa） Fragment：RESIDUES 21-319	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MAN alpha-D-mannopyranose × 11 IOD IODIDE ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions pH 3.6；20 % PEG 3350, 50 MM NAI, 0.1 M SODIUM CITRATE PH 3.6	Resolution 1.15 Å R-free 0.171
2CIX chloroperoxidase complexed with cyclopentanedione Deposited 2006-03-26	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 21–319（299 aa） Fragment：RESIDUES 21-319	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MAN alpha-D-mannopyranose × 10 EDO 1,2-ETHANEDIOL × 1 CEJ CYCLOPENTANE-1,3-DIONE × 1 BR BROMIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 3.6；ML: 22 % PEG3000, 0.1 M KBR, 0.1 M CITRATE PH 3.6 CRYSTALS WERE SOAKED IN ML SUPPLEMENTED WITH 200 MM CYCLOPENTANEDIONE, 10 % DMSO	Resolution 1.80 Å R-free 0.217
2CIY Chloroperoxidase complexed with cyanide and DMSO Deposited 2006-03-26	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 21–319（299 aa） Fragment：RESIDUES 21-319	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MAN alpha-D-mannopyranose × 11 BR BROMIDE ION × 2 EDO 1,2-ETHANEDIOL × 1 CYN CYANIDE ION × 1 DMS DIMETHYL SULFOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；CRYSTALLISATION CONDITIONS: 22 % PEG 3000, 0.1 M KBR, 0.1 M CITRATE PH 3.6 CRYSTALS WERE SOAKED IN 50 MM KCN, 200 MM CYCLOPENTANEDIONE, 10 % DMSO, 22 % PEG3000, 0.1 M SODIUM CITRATE PH 6 FOR 10 MIN AT ROOM TMEPERATURE	Resolution 1.70 Å R-free 0.204
2CIZ chloroperoxidase complexed with acetate Deposited 2006-03-26	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 21–319（299 aa） Fragment：RESIDUES 21-319	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MAN alpha-D-mannopyranose × 9 EDO 1,2-ETHANEDIOL × 2 ACT ACETATE ION × 2 BR BROMIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 3.6；CRYSTALS WERE SOAKED IN 300 MM ACETIC ACID, 50 MM KBR, 22 % PEG3000, 0.1 M CITRATE PH 3.6 FOR 10 MIN AT ROOM TEMPERATURE	Resolution 1.30 Å R-free 0.170
2CJ0 chloroperoxidase complexed with nitrate Deposited 2006-03-26	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 21–319（299 aa） Fragment：RESIDUES 21-319	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MAN alpha-D-mannopyranose × 12 EDO 1,2-ETHANEDIOL × 3 NO3 NITRATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions 50 MM MG(NO3)2, 20 % PEG 3000, 0.1 M SODIUM CITRATE PH3.6	Resolution 1.75 Å R-free 0.207
2CJ2 chloroperoxidase complexed with formate (sugar cryoprotectant) Deposited 2006-03-26	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 21–319（299 aa） Fragment：RESIDUES 21-319	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MAN alpha-D-mannopyranose × 10 FMT FORMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 3.6；100 MM SODIUM FORMATE, 24 % PEG 3000, 0.1 M SODIUM CITRATE PH 3.6 CRYOPROTECTANT: ML SUPPLEMENTED WITH 10 % XYLITOL, 10 % SUCROSE	Resolution 1.60 Å R-free 0.204
2CPO CHLOROPEROXIDASE Deposited 1996-02-10	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 22–319（298 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MAN alpha-D-mannopyranose × 8 MN MANGANESE (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å R-free 0.228
2J18 Chloroperoxidase mixture of ferric and ferrous states (low dose data set) Deposited 2006-08-09	Different construct 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 22–319（298 aa） Fragment：RESIDUES 22-319	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MAN alpha-D-mannopyranose × 9 BR BROMIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 3.4；50MM KBR, 20% PEG3000, 0.1 M SODIUM CITRATE PH3.4, pH 3.40	Resolution 1.75 Å R-free 0.206
2J19 Ferrous Chloroperoxidase (high dose data set) Deposited 2006-08-09	Different construct 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 22–319（298 aa） Fragment：RESIDUES 22-319	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MAN alpha-D-mannopyranose × 9 BR BROMIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 3.4；50MM KBR, 20% PEG3000, 0.1 SODIUM CITRATE PH 3.4	Resolution 1.75 Å R-free 0.204
2J5M Structure of Chloroperoxidase Compound 0 Deposited 2006-09-18	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 21–319（299 aa） Fragment：RESIDUES 21-319	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 PEO HYDROGEN PEROXIDE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MAN alpha-D-mannopyranose × 10 EDO 1,2-ETHANEDIOL × 1 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；22 % PEG3000, 0.1 M KBR, 0.1 M NA CITRATE PH 3.6	Resolution 1.75 Å R-free 0.210
7RST The Crystal Structure of Recombinant Chloroperoxidase Expressed in Aspergillus niger Deposited 2021-08-11	Different construct 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 21–319（299 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MAN alpha-D-mannopyranose × 12 IOD IODIDE ION × 10	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；0.2M NaI, 20% polyethyleneglycol (PEG) 3350	Resolution 1.69 Å R-free 0.210

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

View Construct and Data Evidence

UniProt name	PRXC_CALFU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–299； UniProt 21–319

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2cj1
Deposition date deposition_date	2006-03-26
Structure title title	chloroperoxidase complexed with formate (ethylene glycol cryoprotectant)
Keywords keywords	OXIDOREDUCTASE, HEME, IRON, CHLORIDE, MANGANESE, PEROXIDASE, PYRROLIDONE CARBOXYLIC ACID, GLYCOPROTEIN, METAL-BINDING; OXIDOREDUCTASE
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	19.76 Å
Radius of gyration Rg (electron density) rg_electron	18.53 Å
Forward intensity I(0) i0	23721500.00
Molecular weight molecular_weight	36706.0 kDa
Excluded volume excluded_volume	45491 Å³
Envelope volume envelope_volume	50327 Å³
Hydration-shell volume shell_volume	21852 Å³
Envelope diameter envelope_diameter	64.2 Å
Shell Rg shell_rg	25.78 Å
Envelope Rg envelope_rg	18.96 Å
Shape Rg shape_rg	18.50 Å
Total Rg total_rg	19.54 Å
Total atoms total_atoms	2585
Residues n_residues	298
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	61.6 Å
Rg (real space) rg_real	19.60 Å
Rg uncertainty (real space) rg_real_error	0.29 Å
I(0) (real space) i0_real	2.3720e+07
I(0) uncertainty (real space) i0_real_error	2.5450e+05
Rg (reciprocal space) rg_reciprocal	19.62 Å
I(0) (reciprocal space) i0_reciprocal	23720000.0000
Solution quality estimate total_estimate	0.7418
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.0 Å
Skewness Skewness skewness	0.115
Kurtosis Kurtosis kurtosis	-0.446
Angular range angular_range	— – 0.4000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	5898000.0000
Real-space data points n_real_points	72
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 0.338; Positv: 1.000; Valcen: 0.991; Smooth: 0.961

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (10)

Entity 1 Entity 1 polymer

Description description	CHLOROPEROXIDASE
Molecular weight formula_weight	32746.9 kDa
EC 编号 ec_number	1.11.1.10
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2965

QEPGSGIGYPYDNNTLPYVAPGPTDSRAPCPALNALANHGYIPHDGRAISRETLQNAFLNHMGIANSVIELALTNAFVVCEYVTGSDCGDSLVNLTLLAEPHAFEHDHSFSRKDYKQGVANSNDFIDNRNFDAETFQTSLDVVAGKTHFDYADMNEIRLQRESLSNELDFPGWFTESKPIQNVESGFIFALVSDFNLPDNDENPLVRIDWWKYWFTNESFPYHLGWHPPSPAREIEFVTSASSAVLAASVTSTPSSLPSGAIGPGAEAVPLSFASTMTPFLLATNAPYYAQDPTLGPND

Entity 2 Entity 2 branched

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	424.4 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 branched

Description description	alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose
Molecular weight formula_weight	342.3 kDa
Source method src_method	man
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	MANGANESE (II) ION
Molecular weight formula_weight	54.9 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 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 6 Entity 6 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	2

Entity 7 Entity 7 non-polymer

Description description	alpha-D-mannopyranose
Molecular weight formula_weight	180.2 kDa
Source method src_method	man
Copy count entity_count	12

Entity 8 Entity 8 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 9 Entity 9 non-polymer

Description description	FORMIC ACID
Molecular weight formula_weight	46.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 10 Entity 10 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	349

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2cj1a1
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.3 — Cloroperoxidase
Family Family family	a.39.3.1 — Cloroperoxidase

Domain ID domain_id	d2cj1a2
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.3 — Cloroperoxidase
Family Family family	a.39.3.1 — Cloroperoxidase

CATH v4.4 (1 domains)

Domain ID domain_id	2cj1A00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	489 — Chloroperoxidase
Homologous superfamily homologous superfamily	10 — Chloroperoxidase-like

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8. Citations (1)

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Unit-cell length a length_a	58.280 Å
Unit-cell length b length_b	150.330 Å
Unit-cell length c length_c	99.690 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	1.700 Å
Low-resolution limit resolution_low	19.750 Å
R factor r_factor	0.1910
R_work r_work	0.1890
R_free r_free	0.2290

fit	/app/data/saxs_computation/cj/2cj1/2cj1.fit
pddf	/app/data/pr_computation/cj/2cj1/2cj1.pr.out
profile	/app/data/saxs_computation/cj/2cj1/2cj1.dat

chloroperoxidase complexed with formate (ethylene glycol cryoprotectant)