3h40

Binary complex of human DNA polymerase iota with template U/T

Method: X-RAY DIFFRACTION Dmax: 77.3 Å Quality: GOOD

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

DNA polymerase iota

Homo sapiens

UniProt Q9UNA4

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 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 26–414 Fragment:UNP residues 26-414, UmuC domain, DNA binding domain 5'-D(*TP*(BRU)P*GP*GP*GP*TP*CP*CP*T)-3' × 1 5'-D(*AP*GP*GP*AP*CP*CP*(DOC))-3' × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;10-15 % PEG 5K MME, 0.2-0.4 M Ammonium sulfate, 0.1 M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K Resolution 2.30 Å R-free 0.277

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.

52 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLI_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–389; UniProt 26–414

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 3h40

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3h40
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3h40
Deposition date deposition_date2009-04-17
Structure title titleBinary complex of human DNA polymerase iota with template U/T
Keywords keywords;DNA polymerase iota, replication, DNA damage, DNA repair, DNA replication, DNA synthesis, DNA-binding, DNA-directed DNA polymerase, Magnesium, Metal-binding, Mutator protein, Nucleotidyltransferase, Nucleus, Schiff base, Transferase, REPLICATION-DNA COMPLEX ;; REPLICATION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.23
Radius of gyration Rg (electron density) rg_electron22.83
Forward intensity I(0) i039674200.00
Molecular weight molecular_weight44921.0 kDa
Excluded volume excluded_volume54680 ų
Envelope volume envelope_volume68675 ų
Hydration-shell volume shell_volume25268 ų
Envelope diameter envelope_diameter80.5
Shell Rg shell_rg29.71
Envelope Rg envelope_rg22.89
Shape Rg shape_rg22.85
Total Rg total_rg23.56
Total atoms total_atoms3125
Residues n_residues386
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 dmax77.3
Rg (real space) rg_real23.16
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real3.9670e+07
I(0) uncertainty (real space) i0_real_error5.7080e+05
Rg (reciprocal space) rg_reciprocal23.18
I(0) (reciprocal space) i0_reciprocal39670000.0000
Solution quality estimate total_estimate0.8061
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.292
Kurtosis Kurtosis kurtosis-0.262
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10630000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.826; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3h40a1
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.8 — DNA/RNA polymerases
Superfamily Superfamily superfamilye.8.1 — DNA/RNA polymerases
Family Family familye.8.1.7 — Lesion bypass DNA polymerase (Y-family), catalytic domain
Domain ID domain_idd3h40a2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.240 — Lesion bypass DNA polymerase (Y-family), little finger domain
Superfamily Superfamily superfamilyd.240.1 — Lesion bypass DNA polymerase (Y-family), little finger domain
Family Family familyd.240.1.1 — Lesion bypass DNA polymerase (Y-family), little finger domain

CATH v4.4 (4 domains)

Domain ID domain_id3h40A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily270 — Reverse transcriptase/Diguanylate cyclase domain
Domain ID domain_id3h40A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1170 — MutS, DNA mismatch repair protein, domain I
Homologous superfamily homologous superfamily60
Domain ID domain_id3h40A03
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_id3h40A04
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily100 — DNA polymerase, Y-family, little finger domain

8. Citations (1)

9. Files and Curves (10)