6kfp

Crystal structure of MavC ternary complex

Method: X-RAY DIFFRACTION Dmax: 82.8 Å Quality: EXCELLENT

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

MavC

Legionella pneumophila

UniProt A0A2S6F4I5

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 7–384 Mutation:C74A Ubiquitin-conjugating enzyme E2 N × 1 (P61088) Ubiquitin-40S ribosomal protein S27a × 1 (J3QTR3) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;PEG 3350, lithium chloride Resolution 2.92 Å R-free 0.250

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.

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

View Construct and Data Evidence
UniProt name A0A2S6F4I5_LEGPN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–378; UniProt 7–384

Ubiquitin-conjugating enzyme E2 N

Homo sapiens

UniProt P61088

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 B; UniProt 1–152 Not recorded MavC × 1 (A0A2S6F4I5) Ubiquitin-40S ribosomal protein S27a × 1 (J3QTR3) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;PEG 3350, lithium chloride Resolution 2.92 Å R-free 0.250

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.

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

View Construct and Data Evidence
UniProt name UBE2N_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–152; UniProt 1–152

Ubiquitin-40S ribosomal protein S27a

Homo sapiens

UniProt J3QTR3

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 1–76 Not recorded MavC × 1 (A0A2S6F4I5) Ubiquitin-conjugating enzyme E2 N × 1 (P61088) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;PEG 3350, lithium chloride Resolution 2.92 Å R-free 0.250

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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name J3QTR3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 2–77; UniProt 1–76

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 6kfp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6kfp
Deposition date deposition_date2019-07-08
Structure title titleCrystal structure of MavC ternary complex
Keywords keywordsdeamidase, complex, ANTITOXIN, ANTITOXIN-TRANSFERASE complex; ANTITOXIN/TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.39
Radius of gyration Rg (electron density) rg_electron26.17
Forward intensity I(0) i074095600.00
Molecular weight molecular_weight67556.0 kDa
Excluded volume excluded_volume84845 ų
Envelope volume envelope_volume106280 ų
Hydration-shell volume shell_volume33585 ų
Envelope diameter envelope_diameter87.5
Shell Rg shell_rg33.80
Envelope Rg envelope_rg25.94
Shape Rg shape_rg26.16
Total Rg total_rg27.07
Total atoms total_atoms4753
Residues n_residues596
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 dmax82.8
Rg (real space) rg_real27.23
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real7.4100e+07
I(0) uncertainty (real space) i0_real_error1.0470e+06
Rg (reciprocal space) rg_reciprocal27.28
I(0) (reciprocal space) i0_reciprocal74100000.0000
Solution quality estimate total_estimate0.9106
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.7
Skewness Skewness skewness0.130
Kurtosis Kurtosis kurtosis-0.539
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13580000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.962; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd6kfpb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.20 — UBC-like
Superfamily Superfamily superfamilyd.20.1 — UBC-like
Family Family familyd.20.1.1 — UBC-related
Domain ID domain_idd6kfpd1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related
Domain ID domain_idd6kfpd2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

8. Citations (1)

9. Files and Curves (10)