Research workbench
Solution structure of xpc binding domain of HHR23B
Analyse Solution structure of xpc binding domain of HHR23B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PVE
- Type
- protein
- Length
- 72 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- UV excision repair protein RAD23 homolog B
- UniProt
- P54727
Structure
solution nmr · 1 distinct chain · 57% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UV excision repair protein RAD23 homolog B | protein | 72 | 57% helix, 0% strand | P54727 |
Compared structures
- 1PVE · Solution structure of XPC binding domain of hHR23B · the same entry in another collection · chain A against A, TM-score 1.00
- P54727 · AlphaFold monomer V2.0 prediction for UV excision repair protein RAD23 homolog B (P54727) · a predicted model of the same protein · chain A against A, TM-score 0.77
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 P54727
- Elsewhere: RCSB PDB 1PVE · PDBe 1PVE · UniProt P54727
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