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1arx

CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS

Method: X-RAY DIFFRACTION Dmax: 65.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PEROXIDASE

OrganismNot specified

UniProt P28313

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 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 21–364 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 2 IOD IODIDE ION × 7 K POTASSIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；pH 6.5 Resolution 1.90 Å

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 1ARX Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1ARP Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 angstroms resolution: structural comparisons with the lignin and cytochrome C peroxidases Deposited 1993-06-18 Different ligand/ion Different experimental conditions Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–364（344 aa）
Not recorded CA CALCIUM ION × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.90 Å
1ARU CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS Deposited 1995-04-25 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–364（344 aa）
Not recorded CYN CYANIDE ION × 1 CA CALCIUM ION × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 1.60 Å
1ARV CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS Deposited 1995-04-25 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–364（344 aa）
Not recorded CYN CYANIDE ION × 1 CA CALCIUM ION × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5；pH 5.0
Resolution 1.60 Å
1ARW CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS Deposited 1995-04-25 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–364（344 aa）
Not recorded CYN CYANIDE ION × 1 CA CALCIUM ION × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4；pH 4.0
Resolution 1.60 Å
1ARY CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS Deposited 1995-04-25 Different experimental conditions Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–364（344 aa）
Not recorded CA CALCIUM ION × 2 IOD IODIDE ION × 7 K POTASSIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5；pH 5.0
Resolution 1.90 Å
1C8I BINDING MODE OF HYDROXYLAMINE TO ARTHROMYCES RAMOSUS PEROXIDASE Deposited 2000-05-08 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–364（344 aa）
Not recorded BMA beta-D-mannopyranose × 1 CA CALCIUM ION × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 HOA HYDROXYAMINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.6；pH 5.6
Resolution 2.00 Å R-free 0.223
1CK6 BINDING MODE OF SALICYLHYDROXAMIC ACID TO ARTHROMYCES RAMOSUS PEROXIDASE Deposited 1999-04-28 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 36–364（329 aa）
Not recorded BMA beta-D-mannopyranose × 1 CA CALCIUM ION × 2 SHA SALICYLHYDROXAMIC ACID × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.5；pH 5.5
Resolution 1.90 Å R-free 0.228
1GZA PEROXIDASE Deposited 1996-11-13 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–364（344 aa）
Not recorded CA CALCIUM ION × 2 IOD IODIDE ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.5；pH 5.5
Resolution 2.06 Å
1GZB PEROXIDASE Deposited 1996-11-13 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–364（344 aa）
Not recorded CA CALCIUM ION × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.5；pH 4.5
Resolution 1.80 Å
1HSR BINDING MODE OF BENZHYDROXAMIC ACID TO ARTHROMYCES RAMOSUS PEROXIDASE Deposited 1997-07-01 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–364（344 aa）
Not recorded CA CALCIUM ION × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 BHO BENZHYDROXAMIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.5；pH 5.5
Resolution 1.60 Å
2E39 Crystal structure of the CN-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution Deposited 2006-11-22 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–364（344 aa）
Not recorded MAN alpha-D-mannopyranose × 1 CA CALCIUM ION × 2 CYN CYANIDE ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICRODIALYSIS；pH 7.5；297 K；37% saturated ammonium sulfate, Tris-HCl, pH 7.5, MICRODIALYSIS, temperature 297K
Resolution 1.30 Å R-free 0.203
2E3A Crystal structure of the NO-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution Deposited 2006-11-22 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–364（344 aa）
Not recorded MAN alpha-D-mannopyranose × 1 CA CALCIUM ION × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NO NITRIC OXIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICRODIALYSIS；pH 7.5；297 K；37% saturated ammonium sulfate, Tris-HCl, pH 7.5, MICRODIALYSIS, temperature 297K
Resolution 1.30 Å R-free 0.201
2E3B Crystal structure of the HA-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution Deposited 2006-11-22 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–364（344 aa）
Not recorded MAN alpha-D-mannopyranose × 1 CA CALCIUM ION × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 HOA HYDROXYAMINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICRODIALYSIS；pH 7.5；297 K；37% saturated ammonium sulfate, Tris-HCl, pH 7.5, MICRODIALYSIS, temperature 297K
Resolution 1.30 Å R-free 0.199

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

View Construct and Data Evidence
UniProt name PER_ARTRA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–344； UniProt 21–364

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 1arx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1arx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1arx
Deposition date deposition_date1995-04-25
Structure title titleCRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS
Keywords keywordsPEROXIDASE (DONOR:H2O2 OXIDOREDUCTASE); PEROXIDASE (DONOR:H2O2 OXIDOREDUCTASE)
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_guinier20.24 Å
Radius of gyration Rg (electron density) rg_electron19.37 Å
Forward intensity I(0) i026543100.00
Molecular weight molecular_weight37150.0 kDa
Excluded volume excluded_volume45167 ų
Envelope volume envelope_volume50583 ų
Hydration-shell volume shell_volume21557 ų
Envelope diameter envelope_diameter67.0 Å
Shell Rg shell_rg26.13 Å
Envelope Rg envelope_rg19.78 Å
Shape Rg shape_rg19.45 Å
Total Rg total_rg19.99 Å
Total atoms total_atoms2546
Residues n_residues336
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 dmax65.3 Å
Rg (real space) rg_real20.16 Å
Rg uncertainty (real space) rg_real_error0.36 Å
I(0) (real space) i0_real2.6540e+07
I(0) uncertainty (real space) i0_real_error3.0500e+05
Rg (reciprocal space) rg_reciprocal20.18 Å
I(0) (reciprocal space) i0_reciprocal26540000.0000
Solution quality estimate total_estimate0.8844
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.2 Å
Skewness Skewness skewness0.270
Kurtosis Kurtosis kurtosis-0.288
Angular range angular_range— – 0.3950 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3934000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.954
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1arxa_
Class classa — All alpha proteins
Fold Fold folda.93 — Heme-dependent peroxidases
Superfamily Superfamily superfamilya.93.1 — Heme-dependent peroxidases
Family Family familya.93.1.1 — CCP-like

CATH v4.4 (2 domains)

Domain ID domain_id1arxA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10 —
Domain ID domain_id1arxA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology420 — Peroxidase; domain 2
Homologous superfamily homologous superfamily10 — Peroxidase, domain 2
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8. Citations (3)

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9. Files and Curves (10)