5lod

Crystal structure of HhaI DNA methyltransferase in APO form

Method: X-RAY DIFFRACTION Dmax: 107.5 Å Quality: GOOD

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

Modification methylase HhaI

Haemophilus parahaemolyticus

UniProt P05102

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–327 Chain B; UniProt 1–327 Not recorded SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;AMMONIUM SULFATE 50 mM, CITRATE 100mM, 32% (w/v) PEG-4000 Resolution 1.90 Å R-free 0.219

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.

30 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MTH1_HAEPH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–327; UniProt 1–327 Author chain B; PDBConstruct 1–327; UniProt 1–327

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 5lod

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5lod
Deposition date deposition_date2016-08-09
Structure title titleCrystal structure of HhaI DNA methyltransferase in APO form
Keywords keywordsM.HhaI, C5-METHYLCYTOSINE, APO FORM, DNA methyltransferase, transferase; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.53
Radius of gyration Rg (electron density) rg_electron29.03
Forward intensity I(0) i085859200.00
Molecular weight molecular_weight73187.0 kDa
Excluded volume excluded_volume91599 ų
Envelope volume envelope_volume110640 ų
Hydration-shell volume shell_volume32893 ų
Envelope diameter envelope_diameter119.0
Shell Rg shell_rg35.06
Envelope Rg envelope_rg28.94
Shape Rg shape_rg29.05
Total Rg total_rg29.52
Total atoms total_atoms5147
Residues n_residues642
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 dmax107.5
Rg (real space) rg_real29.65
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real8.5860e+07
I(0) uncertainty (real space) i0_real_error1.4020e+06
Rg (reciprocal space) rg_reciprocal29.60
I(0) (reciprocal space) i0_reciprocal85860000.0000
Solution quality estimate total_estimate0.7574
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.491
Kurtosis Kurtosis kurtosis-0.197
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24820000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.653; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.888; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5loda_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.66 — S-adenosyl-L-methionine-dependent methyltransferases
Superfamily Superfamily superfamilyc.66.1 — S-adenosyl-L-methionine-dependent methyltransferases
Family Family familyc.66.1.26 — C5 cytosine-specific DNA methylase, DCM
Domain ID domain_idd5lodb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.66 — S-adenosyl-L-methionine-dependent methyltransferases
Superfamily Superfamily superfamilyc.66.1 — S-adenosyl-L-methionine-dependent methyltransferases
Family Family familyc.66.1.26 — C5 cytosine-specific DNA methylase, DCM

CATH v4.4 (4 domains)

Domain ID domain_id5lodA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39
Domain ID domain_id5lodA02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology120 — DNA Methylase; Chain A, domain 2
Homologous superfamily homologous superfamily10 — DNA Methylase, subunit A, domain 2
Domain ID domain_id5lodB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39
Domain ID domain_id5lodB02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology120 — DNA Methylase; Chain A, domain 2
Homologous superfamily homologous superfamily10 — DNA Methylase, subunit A, domain 2

8. Citations (1)

9. Files and Curves (10)