Research workbench
The structure of sfaa
Analyse The structure of sfaa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L86
- Type
- protein
- Length
- 1,158 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A2H4T920
- Ligands
- LMR, MLT, FE2
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 292 | — | A0A2H4T920 |
| B | — | protein | 287 | — | A0A2H4T920 |
| C | — | protein | 290 | — | A0A2H4T920 |
| D | — | protein | 289 | — | A0A2H4T920 |
Ligands and binding sites
- LMR · (2S)-2-hydroxybutanedioic acid · ligand · 5 copies · chains A, B, C, D
- MLT · D-malate · ligand · chains A
- FE2 · Fe (II) ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6L86 · The structure of SfaA · the same entry in another collection · chain C against C, 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 A0A2H4T920
- Elsewhere: RCSB PDB 6L86 · PDBe 6L86 · UniProt A0A2H4T920
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