Research workbench
Structural and functional studies of helicobacter pylori wild-type and mutated proteins phosphopantetheine adenylyltransferase
Analyse Structural and functional studies of helicobacter pylori wild-type and mutated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OTW
- Type
- protein
- Length
- 937 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O26010
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 157 | — | O26010 |
| B, C, D, E, F | — | protein | 156 | — | O26010 |
Compared structures
- 3OTW · Structural and Functional Studies of Helicobacter pylori Wild-Type and Mutated Proteins… · the same entry in another collection · chain F against F, TM-score 1.00
- O26010 · AlphaFold monomer V2.0 prediction for phosphopantetheine adenylyltransferase (O26010) · a predicted model of the same protein · chain E against A, TM-score 0.97
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 O26010
- Elsewhere: RCSB PDB 3OTW · PDBe 3OTW · UniProt O26010
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