Research workbench
Acinetobacter sp. tol 5 ataa N-terminal half of C-terminal stalk fused to GCN4 adaptors (cstalkn)
Analyse Acinetobacter sp. tol 5 ataa N-terminal half of C-terminal stalk fused to GCN4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WPR
- Type
- protein
- Length
- 650 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trimeric autotransporter adhesin
- UniProt
- K7ZP88
Structure
x-ray diffraction · 3 distinct chains · 42% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trimeric autotransporter adhesin | protein | 225 | 44% helix, 28% strand | K7ZP88 |
| B | Trimeric autotransporter adhesin | protein | 207 | 39% helix, 31% strand | K7ZP88 |
| C | Trimeric autotransporter adhesin | protein | 218 | 42% helix, 29% strand | K7ZP88 |
Interfaces
3 interfaces between chains.
- A–C · 4008 Ų buried · 54 hydrogen bonds · protein-protein
- B–C · 3896 Ų buried · 52 hydrogen bonds · protein-protein
- A–B · 3877 Ų buried · 55 hydrogen bonds · protein-protein
Compared structures
- 3WPR · Acinetobacter sp. Tol 5 AtaA N-terminal half of C-terminal stalk fused to GCN4 adaptors… · 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 K7ZP88
- Elsewhere: RCSB PDB 3WPR · PDBe 3WPR · UniProt K7ZP88
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