MolNFT v1 · #113321 · protein
Complex of the fimh lectin with a C-linked naphtyl alpha-D-mannoside in soaked trigonal crystals at 2.40 a resolution
5ABZ: “Complex of the fimh lectin with a C-linked naphtyl alpha-D-mannoside in soaked trigonal crystals at 2.40 a…”. X-ray diffraction, 2 ligands (Z47, NI), 3 pockets (best druggability 0.52). MolNFT v1 #113321 on GenesisL1: 3D structure…
- PDB
- 5ABZ
- Type
- protein
- Length
- 316 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fimh
- UniProt
- P08191
- Ligands
- Z47, NI
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fimh | protein | 158 | 6% helix, 53% strand | P08191 |
Ligands and binding sites
- Z47 · (2R,3S,4R,5S,6R)-2-(hydroxymethyl)-6-[3-(naphthalen-1-yl)propyl]oxane-3,4,5-triol · ligand · 2 copies · chains A, B
- NI · Nickel (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.52 | 0.86 | 18 | empty |
| 2 | 84 | 0.35 | 0.75 | 22 | empty |
| 3 | 60 | 0.35 | 0.79 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 539 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5ABZ · Complex of the FimH lectin with a C-linked naphtyl alpha-D-mannoside in soaked trigonal… · the same entry in another collection · chain A against A, TM-score 1.00
- P08191 · AlphaFold monomer V2.0 prediction for type 1 fimbrin D-mannose specific adhesin (P08191) · a predicted model of the same protein · chain B against A, TM-score 0.82
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 P08191
- Elsewhere: RCSB PDB 5ABZ · PDBe 5ABZ · UniProt P08191
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