Research workbench
Crystal structure of the ring-H2 domain of arabidopsis RMR1
Analyse Crystal structure of the ring-H2 domain of arabidopsis RMR1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BVW
- Type
- protein
- Length
- 154 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- AT5G66160 protein
- UniProt
- C0Z2X4
- Ligands
- ZN, NA
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | AT5G66160 protein | protein | 79 | 28% helix, 18% strand | C0Z2X4 |
| B | AT5G66160 protein | protein | 75 | 28% helix, 19% strand | C0Z2X4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.31 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 664 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 7BVW · Crystal structure of the RING-H2 domain of Arabidopsis RMR1 · the same entry in another collection · chain A against A, TM-score 1.00
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 C0Z2X4
- Elsewhere: RCSB PDB 7BVW · PDBe 7BVW · UniProt C0Z2X4
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