Research workbench
Crystal structure of thermotoga maritima cheb methylesterase catalytic domain
Analyse Crystal structure of thermotoga maritima cheb methylesterase catalytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SFT
- Type
- protein
- Length
- 189 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chemotaxis response regulator protein-glutamate methylesterase
- EC
- 3.1.1.61
- UniProt
- Q9WYN9
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chemotaxis response regulator protein-glutamate methylesterase (EC 3.1.1.61) | protein | 189 | 34% helix, 26% strand | Q9WYN9 |
Compared structures
- 3SFT · Crystal structure of Thermotoga maritima CheB methylesterase catalytic domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q9WYN9 · AlphaFold monomer V2.0 prediction for protein-glutamate METHYLESTERASE/PROTEIN-glutamine… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9WYN9
- Elsewhere: RCSB PDB 3SFT · PDBe 3SFT · UniProt Q9WYN9
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