Research workbench
Crystal structure of baua, the ferric preacinetobactin receptor from acinetobacter baumannii
Analyse Crystal structure of baua, the ferric preacinetobactin receptor from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HCP
- Type
- protein
- Length
- 2,013 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Baua
- UniProt
- Q76HJ9
- Ligands
- PO4
- Pockets
- 18 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 61% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Baua | protein | 671 | 4% helix, 61% strand | Q76HJ9 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A, B, C
- EDO · 1,2-ethanediol · additive · 71 copies · chains A, B, C
- C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 35 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 456 | 0.87 | 0.95 | 73 | EDO |
| 2 | 421 | 0.86 | 0.94 | 57 | empty |
| 3 | 408 | 0.86 | 0.94 | 58 | EDO |
| 4 | 816 | 0.85 | 0.88 | 113 | EDO, PO4 |
| 5 | 559 | 0.71 | 0.80 | 82 | EDO |
Interfaces
3 interfaces between chains.
- A–B · 733 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 712 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 647 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6HCP · Crystal structure of BauA, the Ferric preacinetobactin receptor from Acinetobacter… · 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 Q76HJ9
- Elsewhere: RCSB PDB 6HCP · PDBe 6HCP · UniProt Q76HJ9
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