5j8c

Human MOF C316S, E350Q crystal structure

Method: X-RAY DIFFRACTION Dmax: 77.0 Å Quality: REASONABLE

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

Histone acetyltransferase KAT8

Homo sapiens

UniProt Q9H7Z6

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 177–458 Fragment:UNP residues 177-458 Mutation:C316S E350Q Non-standard monomer:Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 CL CHLORIDE ION × 2 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;0.2M Ammonium Chloride 28% PEG 3350 0.1M BisTris-HCL pH 6.5 Resolution 2.17 Å R-free 0.234

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.

41 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAT8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 26–307; UniProt 177–458

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 5j8c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5j8c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5j8c
Deposition date deposition_date2016-04-07
Structure title titleHuman MOF C316S, E350Q crystal structure
Keywords keywordsacetyltransferase, MYST, GNAT, epigenetics, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.16
Radius of gyration Rg (electron density) rg_electron20.29
Forward intensity I(0) i014969100.00
Molecular weight molecular_weight30786.0 kDa
Excluded volume excluded_volume39145 ų
Envelope volume envelope_volume45747 ų
Hydration-shell volume shell_volume19610 ų
Envelope diameter envelope_diameter82.6
Shell Rg shell_rg26.22
Envelope Rg envelope_rg20.83
Shape Rg shape_rg20.27
Total Rg total_rg21.23
Total atoms total_atoms2173
Residues n_residues271
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 dmax77.0
Rg (real space) rg_real21.23
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.4970e+07
I(0) uncertainty (real space) i0_real_error1.9830e+05
Rg (reciprocal space) rg_reciprocal21.22
I(0) (reciprocal space) i0_reciprocal14970000.0000
Solution quality estimate total_estimate0.7491
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.492
Kurtosis Kurtosis kurtosis-0.040
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3533000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.620; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.875; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5j8ca1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.108 — Acyl-CoA N-acyltransferases (Nat)
Superfamily Superfamily superfamilyd.108.1 — Acyl-CoA N-acyltransferases (Nat)
Family Family familyd.108.1.0 — automated matches
Domain ID domain_idd5j8ca2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (3 domains)

Domain ID domain_id5j8cA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily60 — N-acetyl transferase-like
Domain ID domain_id5j8cA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily30 — Gcn5-related N-acetyltransferase (GNAT)
Domain ID domain_id5j8cA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

8. Citations (1)

9. Files and Curves (10)