Research workbench
Thermobifida fusca fsch adenylation domain complexed with mbth-like protein fsck and ser-AMP
Analyse Thermobifida fusca fsch adenylation domain complexed with mbth-like protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EA3
- Type
- protein
- Length
- 487 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mbth-like protein; Adenylation domain of fuscachelin synthetase component H
- UniProt
- Q47NS3, Q47NS0
- Ligands
- SRP
- Pockets
- 7 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mbth-like protein | protein | 70 | 33% helix, 27% strand | Q47NS3 |
| B | Adenylation domain of fuscachelin synthetase component H | protein | 417 | 31% helix, 26% strand | Q47NS0 |
Ligands and binding sites
- SRP · Seryl adenylate · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 434 | 0.75 | 0.85 | 60 | SRP |
| 2 | 260 | 0.58 | 0.79 | 29 | empty |
| 3 | 178 | 0.52 | 0.78 | 30 | empty |
| 4 | 57 | 0.47 | 0.85 | 16 | empty |
| 5 | 73 | 0.39 | 0.78 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1137 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 6EA3 · Thermobifida fusca FscH adenylation domain complexed with MbtH-like protein FscK and… · 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 Q47NS3
- Every structure of UniProt Q47NS0
- Elsewhere: RCSB PDB 6EA3 · PDBe 6EA3 · UniProt Q47NS3 · UniProt Q47NS0
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