2pfq

Manganese promotes catalysis in a DNA polymerase lambda-DNA crystal

Method: X-RAY DIFFRACTION Dmax: 72.4 Å Quality: GOOD

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

DNA polymerase lambda

Homo sapiens

UniProt Q9UGP5

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–DNA Monomer Protein × 1 DNA 3 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 242–575 Mutation:C543A Template × 1 Primer × 1 Downstream Primer × 1 MG MAGNESIUM ION × 1 NA SODIUM ION × 2 MN MANGANESE (II) ION × 2 DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE × 1 PPV PYROPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;278 K;10-20% 2-propanol, 0.2 M sodium citrate and 0.1M sodium cacodylate , pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 278K Resolution 2.10 Å R-free 0.287

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.

95 other PDB entries and 142 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOLL_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain A; PDBConstruct 2–335; UniProt 242–575

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 2pfq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2pfq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2pfq
Deposition date deposition_date2007-04-05
Structure title titleManganese promotes catalysis in a DNA polymerase lambda-DNA crystal
Keywords keywordsDNA polymerase, DNA Repair, phosphoryl transfer reaction, manganese, Transferase, lyase-DNA COMPLEX; Transferase, lyase/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.29
Radius of gyration Rg (electron density) rg_electron21.77
Forward intensity I(0) i038787100.00
Molecular weight molecular_weight42460.0 kDa
Excluded volume excluded_volume50684 ų
Envelope volume envelope_volume63053 ų
Hydration-shell volume shell_volume24093 ų
Envelope diameter envelope_diameter73.6
Shell Rg shell_rg28.72
Envelope Rg envelope_rg21.72
Shape Rg shape_rg21.80
Total Rg total_rg22.43
Total atoms total_atoms2954
Residues n_residues346
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 dmax72.4
Rg (real space) rg_real22.20
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real3.8790e+07
I(0) uncertainty (real space) i0_real_error5.7550e+05
Rg (reciprocal space) rg_reciprocal22.22
I(0) (reciprocal space) i0_reciprocal38790000.0000
Solution quality estimate total_estimate0.8922
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.5
Skewness Skewness skewness0.210
Kurtosis Kurtosis kurtosis-0.374
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4196000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2pfqa1
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.6 — DNA polymerase beta, N-terminal domain-like
Family Family familya.60.6.1 — DNA polymerase beta, N-terminal domain-like
Domain ID domain_idd2pfqa2
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.12 — PsbU/PolX domain-like
Family Family familya.60.12.1 — DNA polymerase beta-like, second domain
Domain ID domain_idd2pfqa3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.218 — Nucleotidyltransferase
Superfamily Superfamily superfamilyd.218.1 — Nucleotidyltransferase
Family Family familyd.218.1.2 — DNA polymerase beta-like

CATH v4.4 (4 domains)

Domain ID domain_id2pfqA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily110 — DNA polymerase beta, N-terminal domain-like
Domain ID domain_id2pfqA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily20 — 5' to 3' exonuclease, C-terminal subdomain
Domain ID domain_id2pfqA03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology460 — Beta Polymerase; domain 2
Homologous superfamily homologous superfamily10 — Beta Polymerase, domain 2
Domain ID domain_id2pfqA04
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology210 — Beta Polymerase; domain 3
Homologous superfamily homologous superfamily10 — DNA polymerase, thumb domain

8. Citations (1)

9. Files and Curves (10)