6rxs

Crystal structure of CobB Ac3(A76G,Y92A, I131L, V187Y) in complex with H4K16-Acetyl peptide

Method: X-RAY DIFFRACTION Dmax: 63.4 Å Quality: GOOD

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

NAD-dependent protein deacylase

Escherichia coli (strain K12)

UniProt P75960

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 40–279 Mutation:A76G,Y92A, I131L, V187Y Histone H4 × 1 (P62805) ZN ZINC ION × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;0.1M Bis-Tris, 0.03 M HCl, 23% PEG3350 Resolution 1.60 Å R-free 0.205

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 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NPD_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 15–254; UniProt 40–279

Histone H4

OrganismNot specified

UniProt P62805

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 13–23 Fragment:H4K16Ac Mutation:K16ALY Non-standard monomer:Yes (specific site not provided by mmCIF) NAD-dependent protein deacylase × 1 (P75960) ZN ZINC ION × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;0.1M Bis-Tris, 0.03 M HCl, 23% PEG3350 Resolution 1.60 Å R-free 0.205

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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–11; UniProt 13–23

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 6rxs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6rxs
Deposition date deposition_date2019-06-08
Structure title titleCrystal structure of CobB Ac3(A76G,Y92A, I131L, V187Y) in complex with H4K16-Acetyl peptide
Keywords keywordsdeacylase, NAD, NAD-dependent, hydrolase, Acetyl, Lysine; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.04
Radius of gyration Rg (electron density) rg_electron18.07
Forward intensity I(0) i011731200.00
Molecular weight molecular_weight25161.0 kDa
Excluded volume excluded_volume31362 ų
Envelope volume envelope_volume36133 ų
Hydration-shell volume shell_volume17171 ų
Envelope diameter envelope_diameter66.5
Shell Rg shell_rg23.96
Envelope Rg envelope_rg18.36
Shape Rg shape_rg18.03
Total Rg total_rg19.09
Total atoms total_atoms3516
Residues n_residues225
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 dmax63.4
Rg (real space) rg_real19.00
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real1.1730e+07
I(0) uncertainty (real space) i0_real_error1.4030e+05
Rg (reciprocal space) rg_reciprocal19.01
I(0) (reciprocal space) i0_reciprocal11730000.0000
Solution quality estimate total_estimate0.7996
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.314
Kurtosis Kurtosis kurtosis-0.231
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2000000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.799; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6rxsA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1220 — TPP-binding domain

8. Citations (1)

9. Files and Curves (10)