Research workbench
ABC transporter substrate-binding protein fromdesulfitobacterium hafniense
Analyse ABC transporter substrate-binding protein fromdesulfitobacterium hafniense in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MLC
- Type
- protein
- Length
- 336 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Extracellular ligand-binding receptor
- UniProt
- B8FZ96
- Ligands
- CA, SO4
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Extracellular ligand-binding receptor | protein | 336 | 44% helix, 22% strand | B8FZ96 |
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 | 269 | 0.54 | 0.76 | 40 | SO4 |
| 2 | 55 | 0.32 | 0.77 | 12 | empty |
| 3 | 59 | 0.26 | 0.73 | 16 | empty |
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 4MLC · ABC Transporter Substrate-Binding Protein fromDesulfitobacterium hafniense · 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 B8FZ96
- Elsewhere: RCSB PDB 4MLC · PDBe 4MLC · UniProt B8FZ96
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