Research workbench
Crystal structure of a putative lipoprotein from the DUF903 family (KPN_03160) from klebsiella pneumoniae subsp. pneumoniae mgh 78578 at 2.30 a resolution
Analyse Crystal structure of a putative lipoprotein from the DUF903 family (KPN_03160)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CAI
- Type
- protein
- Length
- 316 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative lipoprotein from the DUF903 family
- UniProt
- A6TD90
- Ligands
- CL
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, F | Putative lipoprotein from the DUF903 family | protein | 53 | 6% helix, 49% strand | A6TD90 |
| C, E | Putative lipoprotein from the DUF903 family | protein | 52 | 6% helix, 50% strand | A6TD90 |
Ligands and binding sites
- CL · Chloride ion · ion · 9 copies · chains A, F, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 820 | 0.67 | 0.75 | 70 | CL |
| 2 | 344 | 0.55 | 0.75 | 37 | CL |
Interfaces
9 interfaces between chains.
- C–D · 630 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 599 Ų buried · 15 hydrogen bonds · protein-protein
- A–E · 555 Ų buried · 12 hydrogen bonds · protein-protein
- C–F · 527 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 123 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
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 A6TD90
- Elsewhere: RCSB PDB 5CAI · PDBe 5CAI · UniProt A6TD90
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