Research workbench
Fimh adhesin-fimc chaperone complex with D-mannose
Analyse Fimh adhesin-fimc chaperone complex with D-mannose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KLF
- Type
- protein
- Length
- 3,872 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein fimc; Fimh protein
- UniProt
- P31697, P08191
- Ligands
- MAN
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K, M, O | Chaperone protein fimc | protein | 205 | 3% helix, 50% strand | P31697 |
| B, D, F, H, J, L, N, P | Fimh protein | protein | 279 | 3% helix, 48% strand | P08191 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 8 copies · chains B, D, F, H, J, L, N, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 983 | 0.77 | 0.79 | 98 | empty |
| 2 | 1123 | 0.77 | 0.79 | 113 | empty |
| 3 | 200 | 0.65 | 0.84 | 32 | empty |
| 4 | 184 | 0.65 | 0.85 | 32 | empty |
| 5 | 192 | 0.63 | 0.83 | 33 | empty |
Interfaces
17 interfaces between chains.
- A–B · 1628 Ų buried · 28 hydrogen bonds · protein-protein
- G–H · 1626 Ų buried · 29 hydrogen bonds · protein-protein
- C–D · 1621 Ų buried · 29 hydrogen bonds · protein-protein
- E–F · 1620 Ų buried · 29 hydrogen bonds · protein-protein
- K–L · 1463 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide (disulfide).
Compared structures
- 1KLF · Fimh adhesin-fimc chaperone complex with D-mannose · the same entry in another collection · chain K against K, TM-score 1.00
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 P31697
- Every structure of UniProt P08191
- Elsewhere: RCSB PDB 1KLF · PDBe 1KLF · UniProt P31697 · UniProt P08191
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