MolNFT v1 · #173470 · protein
Crystal structure of the ternary complex of the E. COLI type 1 pilus proteins fimc, fimi and the N-terminal domain of fimd
7B0X · Chaperone protein fimc: “Crystal structure of the ternary complex of the E. COLI type 1 pilus proteins fimc, fimi and the N-terminal…”. X-ray diffraction, 4 pockets (best druggability 0.62). MolNFT v1 #173470 on GenesisL1: 3D…
- PDB
- 7B0X
- Type
- protein
- Length
- 467 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein fimc; Fimbrin-like protein fimi; Outer membrane usher protein fimd
- UniProt
- P31697, P39264, P30130
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 3 distinct chains · 10% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Chaperone protein fimc | protein | 211 | 5% helix, 52% strand | P31697 |
| I | Fimbrin-like protein fimi | protein | 137 | 5% helix, 41% strand | P39264 |
| D | Outer membrane usher protein fimd | protein | 119 | 24% helix, 30% strand | P30130 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 461 | 0.62 | 0.76 | 47 | empty |
| 2 | 63 | 0.54 | 0.88 | 21 | empty |
| 3 | 62 | 0.37 | 0.79 | 21 | EDO |
| 4 | 60 | 0.37 | 0.79 | 12 | empty |
Interfaces
3 interfaces between chains.
- C–I · 1936 Ų buried · 52 hydrogen bonds · protein-protein
- C–D · 1044 Ų buried · 6 hydrogen bonds · protein-protein
- I–D · 225 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 7B0X · Crystal structure of the ternary complex of the E. coli type 1 pilus proteins FimC, FimI… · the same entry in another collection · chain C against C, TM-score 1.00
- P31697 · AlphaFold monomer V2.0 prediction for chaperone protein fimc (P31697) · a predicted model of the same protein · chain C against A, TM-score 0.96
- P30130 · AlphaFold monomer V2.0 prediction for outer membrane usher protein fimd (P30130) · a predicted model of the same protein · chain D against A, TM-score 0.89
- P39264 · AlphaFold monomer V2.0 prediction for fimbrin-like protein fimi (P39264) · a predicted model of the same protein · chain I against A, TM-score 0.86
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 P39264
- Every structure of UniProt P30130
- Elsewhere: RCSB PDB 7B0X · PDBe 7B0X · UniProt P31697 · UniProt P39264 · UniProt P30130
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