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Structure of a FHBP(V1.4):PORA(P1.16) chimera. fusion at fhbp position 309.

Analyse Structure of a FHBP(V1.4):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: 5NQY
Type: protein
Length: 261 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Factor H binding protein variant B16_001,MAJOR outer membrane protein P.IA,FACTOR H…
UniProt: Q6VS06, P13415
Pockets: 2 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Factor H binding protein variant B16_001,MAJOR outer membrane protein P.IA,FACTOR H binding protein variant B16_001	protein	261	5% helix, 57% strand	Q6VS06, P13415

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.31	0.76	18	empty
2	60	0.29	0.74	12	empty

Compared structures

5NQY · Structure of a fHbp(V1.4):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 0.33

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 Q6VS06
Every structure of UniProt P13415
Elsewhere: RCSB PDB 5NQY · PDBe 5NQY · UniProt Q6VS06 · UniProt P13415

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