MolNFT v1 · #53921 · protein
Crystal structure of G3P from phage IF1 in complex with its coreceptor, the C-terminal domain of tola
2X9A · Attachment protein G3P: “Crystal structure of G3P from phage IF1 in complex with its coreceptor, the C-terminal domain of tola”. X-ray diffraction, 2 pockets (best druggability 0.35). MolNFT v1 #53921 on GenesisL1: 3D structure…
- PDB
- 2X9A
- Type
- protein
- Length
- 302 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Attachment protein G3P; Membrane spanning protein, required for outer membrane integrity
- UniProt
- O80297, Q8X965
- Pockets
- 2 · best druggability 0.35
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Attachment protein G3P | protein | 61 | 8% helix, 62% strand | O80297 |
| B, D | Membrane spanning protein, required for outer membrane integrity | protein | 90 | 44% helix, 23% strand | Q8X965 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.35 | 0.77 | 23 | empty |
| 2 | 51 | 0.29 | 0.76 | 22 | empty |
Interfaces
6 interfaces between chains.
- A–B · 825 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 815 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 439 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 420 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 41 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2X9A · crystal structure of g3p from phage IF1 in complex with its coreceptor, the C-terminal… · 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 O80297
- Every structure of UniProt Q8X965
- Elsewhere: RCSB PDB 2X9A · PDBe 2X9A · UniProt O80297 · UniProt Q8X965
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