Research workbench
Solution structure of the R3H domain from human smubp-2 in complex with 2'-deoxyguanosine-5'-monophosphate
Analyse Solution structure of the R3H domain from human smubp-2 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LRR
- Type
- protein
- Length
- 70 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-binding protein smubp-2
- EC
- 3.6.4.12, 3.6.4.13
- UniProt
- P38935
- Ligands
- DGP
Structure
solution nmr · 1 distinct chain · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-binding protein smubp-2 (EC 3.6.4.12, 3.6.4.13) | protein | 70 | 36% helix, 19% strand | P38935 |
Ligands and binding sites
- DGP · 2'-deoxyguanosine-5'-monophosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2LRR · Solution structure of the R3H domain from human Smubp-2 in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P38935 · AlphaFold monomer V2.0 prediction for DNA-binding protein smubp-2 (P38935) · a predicted model of the same protein · chain A against A, TM-score 0.80
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 P38935
- Elsewhere: RCSB PDB 2LRR · PDBe 2LRR · UniProt P38935
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