6c1p

HypoPP mutant

Method: X-RAY DIFFRACTION Dmax: 109.4 Å Quality: GOOD

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

Ion transport protein

Arcobacter butzleri (strain RM4018)

UniProt A8EVM5

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–267 Chain B; UniProt 1–267 Chain C; UniProt 1–267 Chain D; UniProt 1–267 Mutation:C235I, H123R PO4 PHOSPHATE ION × 2 PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 15 1N7 CHAPSO × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;277 K;ammonium sulphate, Na-citrate Resolution 2.90 Å R-free 0.260

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.

71 other PDB entries and 73 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A8EVM5_ARCB4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 19–285; UniProt 1–267 Author chain B; PDBConstruct 19–285; UniProt 1–267 Author chain C; PDBConstruct 19–285; UniProt 1–267 Author chain D; PDBConstruct 19–285; UniProt 1–267

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 6c1p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6c1p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6c1p
Deposition date deposition_date2018-01-05
Structure title titleHypoPP mutant
Keywords keywordsMutant, METAL TRANSPORT; METAL TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.77
Radius of gyration Rg (electron density) rg_electron32.96
Forward intensity I(0) i0128397000.00
Molecular weight molecular_weight107100.0 kDa
Excluded volume excluded_volume140840 ų
Envelope volume envelope_volume174760 ų
Hydration-shell volume shell_volume44577 ų
Envelope diameter envelope_diameter117.3
Shell Rg shell_rg39.47
Envelope Rg envelope_rg33.24
Shape Rg shape_rg32.97
Total Rg total_rg33.52
Total atoms total_atoms7543
Residues n_residues872
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 dmax109.4
Rg (real space) rg_real33.67
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real1.2840e+08
I(0) uncertainty (real space) i0_real_error2.0820e+06
Rg (reciprocal space) rg_reciprocal33.74
I(0) (reciprocal space) i0_reciprocal128400000.0000
Solution quality estimate total_estimate0.8862
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.2
Skewness Skewness skewness0.213
Kurtosis Kurtosis kurtosis-0.322
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9605000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.886

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd6c1pa_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.14 — Gated ion channels
Superfamily Superfamily superfamilyf.14.1 — Voltage-gated ion channels
Family Family familyf.14.1.2 — Voltage-gated Na/Ca cation channels
Domain ID domain_idd6c1pb_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.14 — Gated ion channels
Superfamily Superfamily superfamilyf.14.1 — Voltage-gated ion channels
Family Family familyf.14.1.2 — Voltage-gated Na/Ca cation channels
Domain ID domain_idd6c1pc_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.14 — Gated ion channels
Superfamily Superfamily superfamilyf.14.1 — Voltage-gated ion channels
Family Family familyf.14.1.2 — Voltage-gated Na/Ca cation channels
Domain ID domain_idd6c1pd_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.14 — Gated ion channels
Superfamily Superfamily superfamilyf.14.1 — Voltage-gated ion channels
Family Family familyf.14.1.2 — Voltage-gated Na/Ca cation channels

8. Citations (2)

9. Files and Curves (10)