Research workbench
Haemophilus influenzae lpoa: monoclinic form (MON2) with 2 molecules per A.U.
Analyse Haemophilus influenzae lpoa: monoclinic form (MON2) with 2 molecules per A.U. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VAT
- Type
- protein
- Length
- 1,082 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Penicillin-binding protein activator lpoa
- UniProt
- P45299
- Pockets
- 10 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Penicillin-binding protein activator lpoa | protein | 540 | 56% helix, 13% strand | P45299 |
| B | Penicillin-binding protein activator lpoa | protein | 542 | 54% helix, 13% strand | P45299 |
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 175 | 0.65 | 0.86 | 24 | empty |
| 2 | 144 | 0.61 | 0.85 | 24 | empty |
| 3 | 394 | 0.61 | 0.77 | 48 | empty |
| 4 | 388 | 0.60 | 0.76 | 44 | empty |
| 5 | 337 | 0.56 | 0.75 | 51 | empty |
Interfaces
1 interface between chains.
- A–B · 471 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 modified, 2 disulfide (engineered, disulfide).
Compared structures
- 5VAT · Haemophilus influenzae LpoA: Monoclinic form (Mon2) with 2 molecules per a.u. · the same entry in another collection · chain A against A, TM-score 1.00
- P45299 · AlphaFold monomer V2.0 prediction for penicillin-binding protein activator lpoa (P45299) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 P45299
- Elsewhere: RCSB PDB 5VAT · PDBe 5VAT · UniProt P45299
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