Research workbench
Bdellovibrio bacteriovorus dgcb fha in complex with phosphorylated N- terminal peptide
Analyse Bdellovibrio bacteriovorus dgcb fha in complex with phosphorylated N- terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HC1
- Type
- protein
- Length
- 216 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ggdef domain protein; Dgcb N-terminus, phosphorylated
- UniProt
- Q6MPU8
- Ligands
- NH2
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ggdef domain protein | protein | 103 | 0% helix, 44% strand | Q6MPU8 |
| B | Ggdef domain protein | protein | 102 | 0% helix, 43% strand | Q6MPU8 |
| C | Dgcb N-terminus, phosphorylated | protein | 11 | 0% helix, 0% strand | — |
Ligands and binding sites
- NH2 · Amino group · ion · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 175 | 0.49 | 0.78 | 32 | empty |
Interfaces
2 interfaces between chains.
- A–B · 553 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 491 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 6HC1 · Bdellovibrio bacteriovorus DgcB FHA in complex with phosphorylated N-terminal peptide · 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 Q6MPU8
- Elsewhere: RCSB PDB 6HC1 · PDBe 6HC1 · UniProt Q6MPU8
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