1d4u

INTERACTIONS OF HUMAN NUCLEOTIDE EXCISION REPAIR PROTEIN XPA WITH RPA70 AND DNA: CHEMICAL SHIFT MAPPING AND 15N NMR RELAXATION STUDIES

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

NUCLEOTIDE EXCISION REPAIR PROTEIN XPA (XPA-MBD)

Homo sapiens

UniProt P23025

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 ZINC ION × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name XPA_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–111; UniProt 40–150

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id1d4u
Deposition date deposition_date1999-10-06
Structure title titleINTERACTIONS OF HUMAN NUCLEOTIDE EXCISION REPAIR PROTEIN XPA WITH RPA70 AND DNA: CHEMICAL SHIFT MAPPING AND 15N NMR RELAXATION STUDIES
Keywords keywordsDNA REPAIR, LOOP-RICH DOMAIN, NMR RELAXATION, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1d4u__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1d4u__assembly_1__model_1 | I(q)

10-2 10-1 105 106 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1d4u__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)17.06 Å
Rg (electron density)15.89 Å
Total Rg16.93 Å
Atom count1832
Residues111
Excluded volume16542 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1d4u__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1d4ua1
Class classa — All alpha proteins
Fold Fold folda.6 — Putative DNA-binding domain
Superfamily Superfamily superfamilya.6.1 — Putative DNA-binding domain
Family Family familya.6.1.2 — DNA repair factor XPA DNA- and RPA-binding domain, C-terminal subdomain
Domain ID domain_idd1d4ua2
Class classg — Small proteins
Fold Fold foldg.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamilyg.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family familyg.39.1.5 — DNA repair factor XPA DNA- and RPA-binding domain, N-terminal subdomain

CATH v4.4 (1 domains)

Domain ID domain_id1d4uA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology530 — Nucleotide Excision Repair Protein XPA (XPA-MBD); B Chain A
Homologous superfamily homologous superfamily10 — XPA C-terminal domain
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7. Citations (1)