Research workbench
Pseudomonas aeruginosa hdah (H143A) unliganded.
Analyse Pseudomonas aeruginosa hdah (H143A) unliganded. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5G13
- Type
- protein
- Length
- 746 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hdah
- UniProt
- Q9HXM1
- Ligands
- K, ZN
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hdah | protein | 370 | 42% helix, 18% strand | Q9HXM1 |
| B | Hdah | protein | 376 | 41% helix, 17% strand | Q9HXM1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 393 | 0.77 | 0.87 | 55 | empty |
| 2 | 157 | 0.69 | 0.89 | 38 | empty |
| 3 | 127 | 0.67 | 0.89 | 26 | empty |
| 4 | 50 | 0.31 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2188 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
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 Q9HXM1
- Elsewhere: RCSB PDB 5G13 · PDBe 5G13 · UniProt Q9HXM1
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