Research workbench
Flagellar protein fcpa from leptospira biflexa / ab-centered monoclinic form
Analyse Flagellar protein fcpa from leptospira biflexa / ab-centered monoclinic form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NQY
- Type
- protein
- Length
- 456 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B0STJ8
- Ligands
- IOD
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 229 | — | B0STJ8 |
| B | — | protein | 227 | — | B0STJ8 |
Ligands and binding sites
- IOD · Iodide ion · ion · 29 copies · chains A, B
- GOL · Glycerol · additive · 4 copies · chains A, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 3 copies · chains B
- PEG · Di(hydroxyethyl)ether · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6NQY · Flagellar protein FcpA from Leptospira biflexa / ab-centered monoclinic form · 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 B0STJ8
- Elsewhere: RCSB PDB 6NQY · PDBe 6NQY · UniProt B0STJ8
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