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Crystal structure of a domain fragment involved in peptide natural product biosynthesis
Analyse Crystal structure of a domain fragment involved in peptide natural product… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TEJ
- Type
- protein
- Length
- 606 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enterobactin synthase component F
- EC
- 2.7.7.-
- UniProt
- P11454
- Pockets
- 6 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enterobactin synthase component F (EC 2.7.7.-) | protein | 320 | 46% helix, 15% strand | P11454 |
| B | Enterobactin synthase component F (EC 2.7.7.-) | protein | 286 | 45% helix, 17% strand | P11454 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.60 | 0.86 | 22 | empty |
| 2 | 198 | 0.52 | 0.77 | 32 | empty |
| 3 | 218 | 0.52 | 0.77 | 31 | empty |
| 4 | 203 | 0.46 | 0.74 | 34 | empty |
| 5 | 83 | 0.39 | 0.78 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 622 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 3TEJ · Crystal structure of a domain fragment involved in peptide natural product biosynthesis · the same entry in another collection · chain B against B, TM-score 1.00
- P11454 · AlphaFold monomer V2.0 prediction for enterobactin synthase component F (P11454) · a predicted model of the same protein · chain B against A, TM-score 0.78
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 P11454
- Elsewhere: RCSB PDB 3TEJ · PDBe 3TEJ · UniProt P11454
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