Research workbench
Solution structure of the TRIM19 B-BOX1 (B1) of human promyelocytic leukemia (pml)
Analyse Solution structure of the TRIM19 B-BOX1 (B1) of human promyelocytic leukemia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MVW
- Type
- protein
- Length
- 102 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein pml
- UniProt
- P29590
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 20% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein pml | protein | 51 | 20% helix, 22% strand | P29590 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 468 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 2MVW · Solution structure of the TRIM19 B-box1 (B1) of human promyelocytic leukemia (PML) · the same entry in another collection · chain A against A, TM-score 1.00
- P29590 · AlphaFold monomer V2.0 prediction for protein pml (P29590) · a predicted model of the same protein · chain A against A, TM-score 0.68
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 P29590
- Elsewhere: RCSB PDB 2MVW · PDBe 2MVW · UniProt P29590
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