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Crystal structure of the neisseria meningitidis factor H binding protein, fhbp (GNA1870) at 2.0 a resolution

Analyse Crystal structure of the neisseria meningitidis factor H binding protein, fhbp… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KVD
Type: protein
Length: 242 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipoprotein
UniProt: Q6QCC2
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 61% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D	Lipoprotein	protein	242	6% helix, 61% strand	Q6QCC2

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	73	0.30	0.73	21	empty

Compared structures

3KVD · Crystal structure of the Neisseria meningitidis Factor H binding protein, fHbp (GNA1870)… · the same entry in another collection · chain D against D, 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 Q6QCC2
Elsewhere: RCSB PDB 3KVD · PDBe 3KVD · UniProt Q6QCC2

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