1lms

Structural model for an alkaline form of ferricytochrome c

Method: SOLUTION NMR Dmax: 45.4 Å Quality: GOOD

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

Cytochrome c, iso-1

Saccharomyces cerevisiae

UniProt P00044

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 1–108 Mutation:K72A,K79A,C102T HEC HEME C × 1 SOLUTION NMR NMR measurement conditions:pH 11.1;298 K;Ionic strength (raw mmCIF value) 50 mM phosphate;Pressure 1 NMR sample composition:2mM protein | 50 mM phosphate buffer; 90% H2O, 10% D2O; pH 11.1 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.

91 other PDB entries and 125 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYC1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–108; UniProt 1–108

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 1lms

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1lms
Deposition date deposition_date2002-05-02
Structure title titleStructural model for an alkaline form of ferricytochrome c
Keywords keywordsalkaline transition; cytochrome c; NMR structure, ELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.40
Radius of gyration Rg (electron density) rg_electron12.94
Forward intensity I(0) i02731480.00
Molecular weight molecular_weight11280.0 kDa
Excluded volume excluded_volume14113 ų
Envelope volume envelope_volume16686 ų
Hydration-shell volume shell_volume10970 ų
Envelope diameter envelope_diameter44.1
Shell Rg shell_rg18.78
Envelope Rg envelope_rg13.35
Shape Rg shape_rg12.89
Total Rg total_rg14.49
Total atoms total_atoms1553
Residues n_residues95
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax45.4
Rg (real space) rg_real14.30
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real2.7310e+06
I(0) uncertainty (real space) i0_real_error2.9350e+04
Rg (reciprocal space) rg_reciprocal14.31
I(0) (reciprocal space) i0_reciprocal2731000.0000
Solution quality estimate total_estimate0.8882
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.4
Skewness Skewness skewness0.099
Kurtosis Kurtosis kurtosis-0.334
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha607600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.857; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1lmsa_
Class classa — All alpha proteins
Fold Fold folda.3 — Cytochrome c
Superfamily Superfamily superfamilya.3.1 — Cytochrome c
Family Family familya.3.1.1 — monodomain cytochrome c

CATH v4.4 (1 domains)

Domain ID domain_id1lmsA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily10 — Cytochrome c-like domain

8. Citations (1)

9. Files and Curves (10)