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1bc9

CYTOHESIN-1/B2-1 SEC7 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE

Method: SOLUTION NMR Dmax: 70.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CYTOHESIN-1

Homo sapiens

UniProt Q15438

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 58–256 Fragment：SEC7 DOMAIN, No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.8；305 K；Ionic strength (raw mmCIF value) 0.47 M；Pressure 1 NMR sample composition：20 MM NAPI, 150 MM (NH4)2SO4, 3MM DTT, 10% D2O 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 1BC9 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4A4P crystal structure of the Sec7 domain from human cytohesin1 Deposited 2011-10-19 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 63–248（186 aa） Fragment：SEC7 DOMAIN, RESIDUES 63-248
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；PEG 3350 12%, AMMONIUM ACETATE 0.4M. GLYCEROL CRYO-PROTECTANT., pH 7
Resolution 2.00 Å R-free 0.222
4A4P crystal structure of the Sec7 domain from human cytohesin1 Deposited 2011-10-19 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 63–248（186 aa） Fragment：SEC7 DOMAIN, RESIDUES 63-248
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；PEG 3350 12%, AMMONIUM ACETATE 0.4M. GLYCEROL CRYO-PROTECTANT., pH 7
Resolution 2.00 Å R-free 0.222

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYH1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–200； UniProt 58–256

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 1bc9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bc9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bc9
Deposition date deposition_date1998-05-06
Structure title titleCYTOHESIN-1/B2-1 SEC7 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
Keywords keywordsEXCHANGE FACTOR, INTEGRIN BINDING PROTEIN; EXCHANGE FACTOR
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier20.93 Å
Radius of gyration Rg (electron density) rg_electron19.67 Å
Forward intensity I(0) i010437400.00
Molecular weight molecular_weight23353.0 kDa
Excluded volume excluded_volume29086 ų
Envelope volume envelope_volume38261 ų
Hydration-shell volume shell_volume17057 ų
Envelope diameter envelope_diameter71.2 Å
Shell Rg shell_rg25.11 Å
Envelope Rg envelope_rg20.13 Å
Shape Rg shape_rg19.59 Å
Total Rg total_rg20.80 Å
Total atoms total_atoms3262
Residues n_residues200
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 dmax70.1 Å
Rg (real space) rg_real20.94 Å
Rg uncertainty (real space) rg_real_error0.46 Å
I(0) (real space) i0_real1.0440e+07
I(0) uncertainty (real space) i0_real_error1.3350e+05
Rg (reciprocal space) rg_reciprocal20.94 Å
I(0) (reciprocal space) i0_reciprocal10440000.0000
Solution quality estimate total_estimate0.8832
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.4 Å
Skewness Skewness skewness0.347
Kurtosis Kurtosis kurtosis-0.360
Angular range angular_range— – 0.3800 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1946000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.849; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.953
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bc9a_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.3 — Sec7 domain
Family Family familya.118.3.1 — Sec7 domain

CATH v4.4 (2 domains)

Domain ID domain_id1bc9A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily20 —
Domain ID domain_id1bc9A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1000 — Arf Nucleotide-binding Site Opener; domain 2
Homologous superfamily homologous superfamily11 — Arf Nucleotide-binding Site Opener,domain 2
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8. Citations (1)

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9. Files and Curves (10)