Research workbench
Crystal structure of phosphatidylserine synthase haemophilus influenzae rd KW20
Analyse Crystal structure of phosphatidylserine synthase haemophilus influenzae rd KW20 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HSI
- Type
- protein
- Length
- 1,346 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylserine synthase
- EC
- 2.7.8.8
- UniProt
- P44704
- Pockets
- 20 · best druggability 0.71
Structure
x-ray diffraction · 3 distinct chains · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylserine synthase (EC 2.7.8.8) | protein | 447 | 41% helix, 21% strand | P44704 |
| B | Phosphatidylserine synthase (EC 2.7.8.8) | protein | 451 | 42% helix, 20% strand | P44704 |
| C | Phosphatidylserine synthase (EC 2.7.8.8) | protein | 448 | 41% helix, 21% strand | P44704 |
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 506 | 0.71 | 0.80 | 49 | empty |
| 2 | 423 | 0.68 | 0.80 | 40 | empty |
| 3 | 435 | 0.68 | 0.80 | 49 | empty |
| 4 | 328 | 0.66 | 0.81 | 40 | empty |
| 5 | 412 | 0.65 | 0.79 | 35 | empty |
Interfaces
3 interfaces between chains.
- A–B · 732 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 645 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 639 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 3HSI · Crystal structure of phosphatidylserine synthase Haemophilus influenzae Rd KW20 · the same entry in another collection · chain A against A, TM-score 1.00
- P44704 · AlphaFold monomer V2.0 prediction for cdp-diacylglycerol--serine… · a predicted model of the same protein · chain C 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 P44704
- Elsewhere: RCSB PDB 3HSI · PDBe 3HSI · UniProt P44704
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