MolNFT v1 · #3844 · protein
Interactions of human nucleotide excision repair protein xpa with RPA70 and DNA: chemical shift mapping and 15N NMR relaxation studies
1D4U · Nucleotide excision repair protein xpa (xpa-mbd): “Interactions of human nucleotide excision repair protein xpa with RPA70 and DNA: chemical shift mapping and…”. Solution nmr, 1 ligand (ZN). MolNFT v1 #3844 on GenesisL1: 3D…
- PDB
- 1D4U
- Type
- protein
- Length
- 111 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleotide excision repair protein xpa (xpa-mbd)
- UniProt
- P23025
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 24% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide excision repair protein xpa (xpa-mbd) | protein | 111 | 24% helix, 11% strand | P23025 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1D4U · Interactions of human nucleotide excision repair protein xpa with RPA70 and DNA: chemical… · the same entry in another collection · chain A against A, TM-score 1.00
- P23025 · AlphaFold monomer V2.0 prediction for DNA repair protein complementing xp-a cells (P23025) · a predicted model of the same protein · chain A against A, TM-score 0.65
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P23025
- Elsewhere: RCSB PDB 1D4U · PDBe 1D4U · UniProt P23025
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