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Meningococcal factor H binding protein mutant L130R/G133D

Analyse Meningococcal factor H binding protein mutant L130R/G133D in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4Z3T
Type: protein
Length: 485 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Factor H binding protein variant A10_001
UniProt: Q6VS32
Ligands: MG
Pockets: 2 · best druggability 0.35

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 63% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Factor H binding protein variant A10_001	protein	249	6% helix, 61% strand	Q6VS32
B	Factor H binding protein variant A10_001	protein	236	7% helix, 65% strand	Q6VS32

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	100	0.35	0.74	21	empty
2	77	0.31	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 60 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4Z3T · Meningococcal Factor H binding protein mutant L130R/G133D · 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 Q6VS32
Elsewhere: RCSB PDB 4Z3T · PDBe 4Z3T · UniProt Q6VS32

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