MolNFT v1 · #29615 · protein
Crystal structure of the ternary complex of fimd (N- terminal domain) with fimc and the pilin domain of fimh
1ZE3 · Chaperone protein fimc: “Crystal structure of the ternary complex of fimd (N- terminal domain) with fimc and the pilin domain of fimh”. X-ray diffraction, 6 pockets (best druggability 0.53). MolNFT v1 #29615 on GenesisL1: 3D…
- PDB
- 1ZE3
- Type
- protein
- Length
- 443 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein fimc; Fimh protein; Outer membrane usher protein fimd
- UniProt
- P31697, P08191, P30130
- Pockets
- 6 · best druggability 0.53
Structure
x-ray diffraction · 3 distinct chains · 9% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Chaperone protein fimc | protein | 205 | 5% helix, 54% strand | P31697 |
| H | Fimh protein | protein | 122 | 0% helix, 48% strand | P08191 |
| D | Outer membrane usher protein fimd | protein | 116 | 23% helix, 34% strand | P30130 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 12 copies · chains C, H, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.53 | 0.86 | 21 | EDO |
| 2 | 99 | 0.48 | 0.81 | 31 | EDO |
| 3 | 174 | 0.45 | 0.75 | 21 | empty |
| 4 | 63 | 0.44 | 0.82 | 14 | empty |
| 5 | 72 | 0.43 | 0.80 | 22 | empty |
Interfaces
3 interfaces between chains.
- C–H · 1539 Ų buried · 34 hydrogen bonds · protein-protein
- C–D · 1123 Ų buried · 12 hydrogen bonds · protein-protein
- H–D · 224 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1ZE3 · Crystal Structure of the Ternary Complex of FIMD (N-Terminal Domain) with FIMC and the… · 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 0.98
- P08191 · AlphaFold monomer V2.0 prediction for type 1 fimbrin D-mannose specific adhesin (P08191) · a predicted model of the same protein · chain H against A, TM-score 0.94
- 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 0.91
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
- Every structure of UniProt P30130
- Elsewhere: RCSB PDB 1ZE3 · PDBe 1ZE3 · UniProt P31697 · UniProt P08191 · UniProt P30130
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