Research workbench
Crystal structure of class 5 fimbriae chaperone cfaa
Analyse Crystal structure of class 5 fimbriae chaperone cfaa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NCD
- Type
- protein
- Length
- 211 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gram-negative pili assembly chaperone, N-terminal domain protein
- UniProt
- N4NNE0
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gram-negative pili assembly chaperone, N-terminal domain protein | protein | 211 | 0% helix, 50% strand | N4NNE0 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.34 | 0.76 | 13 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4NCD · Crystal Structure of Class 5 Fimbriae Chaperone CfaA · the same entry in another collection · chain A against A, 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 N4NNE0
- Elsewhere: RCSB PDB 4NCD · PDBe 4NCD · UniProt N4NNE0
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