Research workbench
Structure of the native moeb-moad protein complex
Analyse Structure of the native moeb-moad protein complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JW9
- Type
- protein
- Length
- 321 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Molybdopterin biosynthesis moeb protein; Molybdopterin [mpt] converting factor, subunit 1
- UniProt
- P12282, P30748
- Ligands
- ZN, SO4
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Molybdopterin biosynthesis moeb protein | protein | 240 | 42% helix, 21% strand | P12282 |
| D | Molybdopterin [mpt] converting factor, subunit 1 | protein | 81 | 27% helix, 27% strand | P30748 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 144 | 0.57 | 0.83 | 34 | SO4 |
| 2 | 120 | 0.43 | 0.76 | 24 | empty |
| 3 | 52 | 0.30 | 0.75 | 12 | empty |
Interfaces
1 interface between chains.
- B–D · 1062 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 1JW9 · Structure of the Native MoeB-MoaD Protein Complex · the same entry in another collection · chain B against B, TM-score 1.00
- P12282 · AlphaFold monomer V2.0 prediction for molybdopterin-synthase adenylyltransferase (P12282) · a predicted model of the same protein · chain B against A, TM-score 0.99
- P30748 · AlphaFold monomer V2.0 prediction for molybdopterin synthase sulfur carrier subunit… · a predicted model of the same protein · chain D against A, TM-score 0.94
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 P12282
- Every structure of UniProt P30748
- Elsewhere: RCSB PDB 1JW9 · PDBe 1JW9 · UniProt P12282 · UniProt P30748
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