Research workbench
Structure of the membrane domains of the sialic acid trap transporter hisiaqm from haemophilus influenzae
Analyse Structure of the membrane domains of the sialic acid trap transporter hisiaqm… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7QE5
- Type
- protein
- Length
- 740 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sialic acid trap transporter permease protein siat; MEGABODY3
- UniProt
- P44543
- Pockets
- 12 · best druggability 0.75
Structure
electron microscopy · 2 distinct chains · 66% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sialic acid trap transporter permease protein siat | protein | 616 | 79% helix, 0% strand | P44543 |
| B | MEGABODY3 | protein | 124 | 2% helix, 31% strand | — |
Pockets
12 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 747 | 0.75 | 0.80 | 79 | empty |
| 2 | 552 | 0.73 | 0.80 | 65 | empty |
| 3 | 181 | 0.68 | 0.87 | 35 | empty |
| 4 | 162 | 0.62 | 0.84 | 28 | empty |
| 5 | 308 | 0.58 | 0.77 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 1109 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7QE5 · Structure of the membrane domains of the sialic acid TRAP transporter HiSiaQM from… · the same entry in another collection · chain A against A, TM-score 1.00
- P44543 · AlphaFold monomer V2.0 prediction for sialic acid trap transporter permease protein siat… · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P44543
- Elsewhere: RCSB PDB 7QE5 · PDBe 7QE5 · UniProt P44543
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