1gx7

Best model of the electron transfer complex between cytochrome c3 and [Fe]-hydrogenase

Dmax: 86.8 Å Quality: REASONABLE

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

PERIPLASMIC [FE] HYDROGENASE LARGE SUBUNIT

OrganismNot specified

UniProt P07598

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 27–397 Not recorded PERIPLASMIC [FE] HYDROGENASE SMALL SUBUNIT × 1 (P07603) CYTOCHROME C3 × 1 (P00131) SF4 IRON/SULFUR CLUSTER × 3 PDT 1,3-PROPANEDITHIOL × 1 FE2 FE (II) ION × 2 CYN CYANIDE ION × 2 CMO CARBON MONOXIDE × 2 HEC HEME C × 4 Experimental method not declared NMR measurement conditions:pH 5.9;296 K;Ionic strength (raw mmCIF value) 10 MM PHOSPHATE BUFFER;Pressure 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.

26 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHFL_DESVH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–371; UniProt 27–397

PERIPLASMIC [FE] HYDROGENASE SMALL SUBUNIT

OrganismNot specified

UniProt P07603

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 36–123 Not recorded PERIPLASMIC [FE] HYDROGENASE LARGE SUBUNIT × 1 (P07598) CYTOCHROME C3 × 1 (P00131) SF4 IRON/SULFUR CLUSTER × 3 PDT 1,3-PROPANEDITHIOL × 1 FE2 FE (II) ION × 2 CYN CYANIDE ION × 2 CMO CARBON MONOXIDE × 2 HEC HEME C × 4 Experimental method not declared NMR measurement conditions:pH 5.9;296 K;Ionic strength (raw mmCIF value) 10 MM PHOSPHATE BUFFER;Pressure 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.

26 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHFS_DESVH
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–88; UniProt 36–123

CYTOCHROME C3

OrganismNot specified

UniProt P00131

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 23–129 Not recorded PERIPLASMIC [FE] HYDROGENASE LARGE SUBUNIT × 1 (P07598) PERIPLASMIC [FE] HYDROGENASE SMALL SUBUNIT × 1 (P07603) SF4 IRON/SULFUR CLUSTER × 3 PDT 1,3-PROPANEDITHIOL × 1 FE2 FE (II) ION × 2 CYN CYANIDE ION × 2 CMO CARBON MONOXIDE × 2 HEC HEME C × 4 Experimental method not declared NMR measurement conditions:pH 5.9;296 K;Ionic strength (raw mmCIF value) 10 MM PHOSPHATE BUFFER;Pressure 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.

5 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYC3_DESVH
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–107; UniProt 23–129

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 1gx7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1gx7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1gx7
Deposition date deposition_date2002-03-28
Structure title titleBest model of the electron transfer complex between cytochrome c3 and [Fe]-hydrogenase
Keywords keywords;OXIDOREDUCTASE, ELECTRON TRANSFER COMPLEX, HYDROGENASE, MULTIHEME CYTOCHROME, SOFT DOCKING, OXIDOREDUCTASE ELECTRON TRANSPORT, 4FE-4S, IRON-SULFUR ;; OXIDOREDUCTASE

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

Radius of gyration Rg (Guinier) rg_guinier24.87
Radius of gyration Rg (electron density) rg_electron24.50
Forward intensity I(0) i073235100.00
Molecular weight molecular_weight65778.0 kDa
Excluded volume excluded_volume81408 ų
Envelope volume envelope_volume89524 ų
Hydration-shell volume shell_volume30208 ų
Envelope diameter envelope_diameter91.9
Shell Rg shell_rg32.23
Envelope Rg envelope_rg25.06
Shape Rg shape_rg24.61
Total Rg total_rg24.92
Total atoms total_atoms5509
Residues n_residues566
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 dmax86.8
Rg (real space) rg_real25.88
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real7.3200e+07
I(0) uncertainty (real space) i0_real_error8.2770e+05
Rg (reciprocal space) rg_reciprocal24.91
I(0) (reciprocal space) i0_reciprocal73230000.0000
Solution quality estimate total_estimate0.6551
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.545
Kurtosis Kurtosis kurtosis-0.038
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha4.5790
Highest regularization parameter α highest_alpha27340000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.785; Stabil: 0.894; Sysdev: 0.000; Positv: 1.000; Valcen: 0.907; Smooth: 0.614

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)