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Crystal structure of human MTR4
Analyse Crystal structure of human MTR4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IEG
- Type
- protein
- Length
- 1,783 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exosome RNA helicase MTR4
- EC
- 3.6.4.13
- UniProt
- P42285
- Ligands
- ADP, MG
- Pockets
- 16 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Exosome RNA helicase MTR4 (EC 3.6.4.13) | protein | 911 | 49% helix, 15% strand | P42285 |
| A | Exosome RNA helicase MTR4 (EC 3.6.4.13) | protein | 872 | 47% helix, 15% strand | P42285 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains B, A
- MG · Magnesium ion · metal · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1006 | 0.76 | 0.78 | 99 | empty |
| 2 | 712 | 0.75 | 0.80 | 80 | empty |
| 3 | 322 | 0.65 | 0.81 | 31 | ADP, MG |
| 4 | 68 | 0.61 | 0.91 | 22 | empty |
| 5 | 215 | 0.60 | 0.81 | 37 | ADP, MG |
Compared structures
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 P42285
- Elsewhere: RCSB PDB 6IEG · PDBe 6IEG · UniProt P42285
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