Research workbench
AlphaFold monomer V2.0 prediction for putative esterase HI_1161 (P45083)
Analyse AlphaFold monomer V2.0 prediction for putative esterase HI_1161 (P45083) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P45083
- Type
- protein
- Length
- 138 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8a7b1782CE62A880494cB63CE2416dfA7aC6391d
- Molecule
- Putative esterase HI_1161
- UniProt
- P45083
Structure
1 distinct chain · 21% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative esterase HI_1161 | protein | 138 | 21% helix, 44% strand | P45083 |
Compared structures
- 3LZ7 · Crystal Structure of thioesterase HI1161 EC3.1.2.- from Haemophilus influenzae.… · an experimental structure of the same protein · chain A against B, TM-score 0.99
- 3LZ7 · Crystal structure of thioesterase HI1161 EC3.1.2.- from haemophilus influenzae.… · an experimental structure of the same protein · chain A against B, TM-score 0.99
- 2B6E · X-ray crystal structure of protein HI1161 from haemophilus influenzae. northeast… · an experimental structure of the same protein · chain A against B, TM-score 0.99
- 2B6E · X-Ray Crystal Structure of Protein HI1161 from Haemophilus influenzae. Northeast… · an experimental structure of the same protein · chain A against B, 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 P45083
- Elsewhere: UniProt P45083 · AlphaFold DB P45083
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