Research workbench
Structure of the ATP-bound moeb-moad protein complex
Analyse Structure of the ATP-bound 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
- 1JWA
- Type
- protein
- Length
- 298 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
- ATP
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Molybdopterin biosynthesis moeb protein | protein | 217 | 43% helix, 24% strand | P12282 |
| D | Molybdopterin [mpt] converting factor, subunit 1 | protein | 81 | 27% helix, 25% strand | P30748 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 175 | 0.57 | 0.81 | 35 | ATP |
| 2 | 224 | 0.55 | 0.78 | 24 | empty |
| 3 | 58 | 0.31 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- B–D · 868 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 1JWA · Structure of the ATP-bound 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 1JWA · PDBe 1JWA · UniProt P12282 · UniProt P30748
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.