Research workbench
Crystal structure of full-length lpoa from haemophilus influenzae at 1.97 ångström resolution
Analyse Crystal structure of full-length lpoa from haemophilus influenzae at 1.97… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KCN
- Type
- protein
- Length
- 538 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Penicillin-binding protein activator lpoa
- UniProt
- P45299
- Ligands
- CL
- Pockets
- 6 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Penicillin-binding protein activator lpoa | protein | 538 | 56% helix, 12% strand | P45299 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.64 | 0.87 | 24 | empty |
| 2 | 312 | 0.57 | 0.76 | 35 | empty |
| 3 | 124 | 0.40 | 0.75 | 18 | empty |
| 4 | 59 | 0.37 | 0.79 | 15 | empty |
| 5 | 57 | 0.29 | 0.75 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5KCN · Crystal Structure of full-length LpoA from Haemophilus influenzae at 1.97 angstrom… · 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 0.97
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 5KCN · PDBe 5KCN · UniProt P45299
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