Research workbench
Fusion of maltose-binding protein and pila from acinetobacter baumannii AB5075
Analyse Fusion of maltose-binding protein and pila from acinetobacter baumannii AB5075 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VAW
- Type
- protein
- Length
- 484 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding periplasmic PROTEIN,TYPE IV pilin pila
- UniProt
- D8A942, A0A0D5YCX7
- Ligands
- GLU, LYS, SER, NA
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose-binding periplasmic PROTEIN,TYPE IV pilin pila | protein | 484 | 41% helix, 19% strand | D8A942, A0A0D5YCX7 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · chains A
- LYS · Lysine · ligand · chains A
- SER · Serine · ligand · chains A
- NA · Sodium ion · metal · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 696 | 0.66 | 0.75 | 62 | MPD, GLU |
| 2 | 217 | 0.53 | 0.77 | 27 | SER |
| 3 | 163 | 0.46 | 0.76 | 30 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5VAW · Fusion of Maltose-binding Protein and PilA from Acinetobacter baumannii AB5075 · 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 D8A942
- Every structure of UniProt A0A0D5YCX7
- Elsewhere: RCSB PDB 5VAW · PDBe 5VAW · UniProt D8A942 · UniProt A0A0D5YCX7
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