Research workbench
Structure of a FHBP(V1.1):PORA(P1.16) chimera. fusion at fhbp position 309.
Analyse Structure of a FHBP(V1.1):PORA(P1.16) chimera. fusion at fhbp position 309. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NQZ
- Type
- protein
- Length
- 530 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9JXV4, P13415
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 267 | — | Q9JXV4, P13415 |
| B | — | protein | 263 | — | Q9JXV4, P13415 |
Ligands and binding sites
- ZN · Zinc ion · metal · 9 copies · chains A, B
- ACT · Acetate ion · additive · 8 copies · chains A, B
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NQZ · Structure of a fHbp(V1.1):PorA(P1.16) chimera. Fusion at fHbp position 309. · the same entry in another collection · chain A against A, TM-score 1.00
- P13415 · AlphaFold monomer V2.0 prediction for major outer membrane protein P.IA (P13415) · a predicted model of the same protein · chain A against A, TM-score 0.35
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 Q9JXV4
- Every structure of UniProt P13415
- Elsewhere: RCSB PDB 5NQZ · PDBe 5NQZ · UniProt Q9JXV4 · UniProt P13415
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