Research workbench
Molybdate bound complex of dimop domain of mode from E.COLI
Analyse Molybdate bound complex of dimop domain of mode from E.COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H9S
- Type
- protein
- Length
- 275 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Molybdenum transport protein mode
- UniProt
- P46930
- Ligands
- MOO
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Molybdenum transport protein mode | protein | 138 | 16% helix, 52% strand | P46930 |
| B | Molybdenum transport protein mode | protein | 137 | 15% helix, 51% strand | P46930 |
Ligands and binding sites
- MOO · Molybdate ion · ion · 2 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 · 1534 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 1H9S · Molybdate bound complex of Dimop domain of ModE from E.coli · 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 P46930
- Elsewhere: RCSB PDB 1H9S · PDBe 1H9S · UniProt P46930
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