11nc

Azotobacter vinelandii MoFeP (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT

Method: ELECTRON MICROSCOPY Dmax: 124.3 Å Quality: GOOD

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

Nitrogenase molybdenum-iron protein alpha chain

OrganismNot specified

UniProt P07328

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–492 Chain C; UniProt 1–492 Not recorded Nitrogenase molybdenum-iron protein beta chain × 2 (P07329) HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Samples were frozen with the SPT Labtech chameleon Resolution 2.16 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.

83 other PDB entries and 89 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NIFD_AZOVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–492; UniProt 1–492 Author chain C; PDBConstruct 1–492; UniProt 1–492

Nitrogenase molybdenum-iron protein beta chain

OrganismNot specified

UniProt P07329

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–523 Chain D; UniProt 1–523 Not recorded Nitrogenase molybdenum-iron protein alpha chain × 2 (P07328) HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Samples were frozen with the SPT Labtech chameleon Resolution 2.16 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.

74 other PDB entries and 81 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NIFK_AZOVI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–523; UniProt 1–523 Author chain D; PDBConstruct 1–523; UniProt 1–523

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 11nc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 11nc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id11nc
Deposition date deposition_date2026-03-05
Structure title titleAzotobacter vinelandii MoFeP (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT
Keywords keywordsNitrogenase, FeMoCo, nitrogen, P-cluster, METAL BINDING PROTEIN, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.53
Radius of gyration Rg (electron density) rg_electron37.92
Forward intensity I(0) i0799580000.00
Molecular weight molecular_weight229830.0 kDa
Excluded volume excluded_volume285910 ų
Envelope volume envelope_volume335720 ų
Hydration-shell volume shell_volume70301 ų
Envelope diameter envelope_diameter126.9
Shell Rg shell_rg46.34
Envelope Rg envelope_rg37.94
Shape Rg shape_rg37.92
Total Rg total_rg38.33
Total atoms total_atoms16021
Residues n_residues1998
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 dmax124.3
Rg (real space) rg_real38.42
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real7.9960e+08
I(0) uncertainty (real space) i0_real_error1.2850e+07
Rg (reciprocal space) rg_reciprocal38.49
I(0) (reciprocal space) i0_reciprocal799600000.0000
Solution quality estimate total_estimate0.8968
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.250
Kurtosis Kurtosis kurtosis-0.544
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha259900000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.950

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)