Research workbench
Crystal structure of thioesterase HI1161 EC3.1.2.- from haemophilus influenzae. orthorombic crystal form. northeast structural genomics consortium target IR63
Analyse Crystal structure of thioesterase HI1161 EC3.1.2.- from haemophilus influenzae.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LZ7
- Type
- protein
- Length
- 567 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative esterase HI1161
- EC
- 3.1.2.-
- UniProt
- P45083
- Pockets
- 5 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 21% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Putative esterase HI1161 (EC 3.1.2.-) | protein | 143 | 20% helix, 41% strand | P45083 |
| B | Putative esterase HI1161 (EC 3.1.2.-) | protein | 140 | 21% helix, 42% strand | P45083 |
| D | Putative esterase HI1161 (EC 3.1.2.-) | protein | 141 | 21% helix, 41% strand | P45083 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · chains A, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 806 | 0.78 | 0.81 | 101 | empty |
| 2 | 343 | 0.70 | 0.82 | 47 | PEG |
| 3 | 499 | 0.69 | 0.79 | 54 | empty |
| 4 | 82 | 0.51 | 0.84 | 20 | empty |
| 5 | 68 | 0.37 | 0.78 | 18 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1266 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1235 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 554 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 550 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 212 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 3LZ7 · Crystal Structure of thioesterase HI1161 EC3.1.2.- from Haemophilus influenzae.… · the same entry in another collection · chain A against A, TM-score 1.00
- P45083 · AlphaFold monomer V2.0 prediction for putative esterase HI_1161 (P45083) · a predicted model of the same protein · chain B against A, TM-score 0.98
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: RCSB PDB 3LZ7 · PDBe 3LZ7 · UniProt P45083
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