Research workbench
Two crystal structures of the cytoplasmic molybdate-binding protein modg suggest a novel cooperative binding mechanism and provide insights into ligand-binding specificity. peg-grown form with molybdate bound
Analyse Two crystal structures of the cytoplasmic molybdate-binding protein modg… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H9M
- Type
- protein
- Length
- 282 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Molybdenum-binding-protein
- UniProt
- Q44529
- Ligands
- MOO
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Molybdenum-binding-protein | protein | 141 | 13% helix, 51% strand | Q44529 |
Ligands and binding sites
- MOO · Molybdate ion · ion · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1H9M · Two crystal structures of the cytoplasmic molybdate-binding protein ModG suggest a novel… · the same entry in another collection · chain B against B, 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 Q44529
- Elsewhere: RCSB PDB 1H9M · PDBe 1H9M · UniProt Q44529
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