Research workbench
Apo hemophilin from a. baumannii
Analyse Apo hemophilin from a. baumannii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RE4
- Type
- protein
- Length
- 722 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemophilin
- UniProt
- N9GH75
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 3 distinct chains · 11% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemophilin | protein | 243 | 10% helix, 53% strand | N9GH75 |
| C | Hemophilin | protein | 240 | 12% helix, 53% strand | N9GH75 |
| E | Hemophilin | protein | 239 | 10% helix, 52% strand | N9GH75 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 348 | 0.55 | 0.75 | 54 | empty |
| 2 | 126 | 0.44 | 0.77 | 29 | empty |
Interfaces
2 interfaces between chains.
- A–C · 461 Ų buried · 7 hydrogen bonds · protein-protein
- A–E · 215 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7RE4 · Apo Hemophilin from A. baumannii · 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 N9GH75
- Elsewhere: RCSB PDB 7RE4 · PDBe 7RE4 · UniProt N9GH75
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