Research workbench
Modbc from methanosarcina acetivorans
Analyse Modbc from methanosarcina acetivorans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D31
- Type
- protein
- Length
- 1,192 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SULFATE/MOLYBDATE ABC transporter, ATP-binding protein; SULFATE/MOLYBDATE ABC…
- UniProt
- Q8TTZ3, Q8TTZ4
- Ligands
- WO4
- Pockets
- 11 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | SULFATE/MOLYBDATE ABC transporter, ATP-binding protein | protein | 348 | 28% helix, 36% strand | Q8TTZ3 |
| C, D | SULFATE/MOLYBDATE ABC transporter, permease protein | protein | 248 | 80% helix, 0% strand | Q8TTZ4 |
Ligands and binding sites
- WO4 · Tungstate(vi)ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 487 | 0.62 | 0.75 | 33 | empty |
| 2 | 208 | 0.58 | 0.80 | 34 | empty |
| 3 | 198 | 0.58 | 0.80 | 33 | empty |
| 4 | 105 | 0.46 | 0.78 | 17 | empty |
| 5 | 181 | 0.46 | 0.75 | 37 | empty |
Interfaces
4 interfaces between chains.
- C–D · 4043 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1262 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 945 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 927 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3D31 · ModBC from Methanosarcina acetivorans · 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 Q8TTZ3
- Every structure of UniProt Q8TTZ4
- Elsewhere: RCSB PDB 3D31 · PDBe 3D31 · UniProt Q8TTZ3 · UniProt Q8TTZ4
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