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1eky

MODEL STRUCTURE FROM NON-NOE BASED NMR STRUCTURE CALCULATION

Method: SOLUTION NMR Dmax: 48.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

;CYTOCHROME C' ;

OrganismNot specified

UniProt P00147

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 1–129 Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 SOLUTION NMR NMR measurement conditions：pH 6；293 K；Ionic strength (raw mmCIF value) 100mM；Pressure ambient NMR sample composition：7mM Cyt c', 15N, 100mM PO4 pH6 | 90% H20 10% D20 Resolution not provided

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 1EKY Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CPQ CYTOCHROME C' FROM RHODOPSEUDOMONAS CAPSULATA Deposited 1995-08-14 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 22–150（129 aa）
Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.72 Å
1CPR ST. LOUIS CYTOCHROME C' FROM THE PURPLE PHOTOTROPIC BACTERIUM, RHODOBACTER CAPSULATUS Deposited 1996-04-09 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 22–150（129 aa）
Not recorded ZN ZINC ION × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.10 Å
1NBB N-BUTYLISOCYANIDE BOUND RHODOBACTER CAPSULATUS CYTOCHROME C' Deposited 1996-03-18 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 22–150（129 aa）
Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NBN N-BUTYL ISOCYANIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 2.40 Å
1NBB N-BUTYLISOCYANIDE BOUND RHODOBACTER CAPSULATUS CYTOCHROME C' Deposited 1996-03-18 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 22–150（129 aa）
Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NBN N-BUTYL ISOCYANIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 2.40 Å
1RCP CYTOCHROME C' Deposited 1995-08-23 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 22–150（129 aa）
Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 2.00 Å
1RCP CYTOCHROME C' Deposited 1995-08-23 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 22–150（129 aa）
Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 2.00 Å

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

View Construct and Data Evidence
UniProt name CYCP_RHOCA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–129； UniProt 1–129

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 1eky

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1eky
Deposition date deposition_date2000-03-10
Structure title titleMODEL STRUCTURE FROM NON-NOE BASED NMR STRUCTURE CALCULATION
Keywords keywordsfour helix bundle, OXYGEN STORAGE-TRANSPORT COMPLEX; OXYGEN STORAGE/TRANSPORT
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.66 Å
Radius of gyration Rg (electron density) rg_electron15.08 Å
Forward intensity I(0) i01657820000.00
Molecular weight molecular_weight285660.0 kDa
Excluded volume excluded_volume330840 ų
Envelope volume envelope_volume27265 ų
Hydration-shell volume shell_volume13832 ų
Envelope diameter envelope_diameter55.9 Å
Shell Rg shell_rg22.51 Å
Envelope Rg envelope_rg17.77 Å
Shape Rg shape_rg15.09 Å
Total Rg total_rg15.14 Å
Total atoms total_atoms28800
Residues n_residues4128
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 dmax48.4 Å
Rg (real space) rg_real14.74 Å
Rg uncertainty (real space) rg_real_error0.36 Å
I(0) (real space) i0_real1.6580e+09
I(0) uncertainty (real space) i0_real_error1.9090e+07
Rg (reciprocal space) rg_reciprocal14.74 Å
I(0) (reciprocal space) i0_reciprocal1658000000.0000
Solution quality estimate total_estimate0.8181
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.1 Å
Skewness Skewness skewness0.444
Kurtosis Kurtosis kurtosis-0.304
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha270100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.603; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.923; Smooth: 0.900
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ekya_
Class classi — Low resolution protein structures
Fold Fold foldi.11 — Computational models partly based on experimental data
Superfamily Superfamily superfamilyi.11.1 — Computational models partly based on experimental data
Family Family familyi.11.1.1 — Computational models partly based on experimental data

CATH v4.4 (1 domains)

Domain ID domain_id1ekyA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily10 — Cytochrome c/b562
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8. Citations (1)

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9. Files and Curves (10)