Research workbench
Mutant N33D structure of phenylacetic acid degradation protein paai from thermus thermophilus HB8
Analyse Mutant N33D structure of phenylacetic acid degradation protein paai from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DSL
- Type
- protein
- Length
- 230 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenylacetic acid degradation protein paai
- UniProt
- Q5SJP3
- Ligands
- MG, CL
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phenylacetic acid degradation protein paai | protein | 115 | 22% helix, 50% strand | Q5SJP3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 640 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2DSL · Mutant N33D structure of phenylacetic acid degradation protein PaaI from Thermus… · 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 Q5SJP3
- Elsewhere: RCSB PDB 2DSL · PDBe 2DSL · UniProt Q5SJP3
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