Research workbench
The fimbrial anchor protein MFA2 from porphyromonas gingivalis
Analyse The fimbrial anchor protein MFA2 from porphyromonas gingivalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NFI
- Type
- protein
- Length
- 277 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Minor fimbrium anchoring subunit MFA2
- UniProt
- B2RHG2
- Ligands
- IOD
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Minor fimbrium anchoring subunit MFA2 | protein | 277 | 3% helix, 49% strand | B2RHG2 |
Ligands and binding sites
- IOD · Iodide ion · ion · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide, 2 modified (disulfide, engineered).
Compared structures
- 5NFI · The fimbrial anchor protein Mfa2 from Porphyromonas gingivalis · the same entry in another collection · chain B against B, TM-score 1.00
- B2RHG2 · AlphaFold monomer V2.0 prediction for minor fimbrium anchoring subunit MFA2 (B2RHG2) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 B2RHG2
- Elsewhere: RCSB PDB 5NFI · PDBe 5NFI · UniProt B2RHG2
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