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Crystal structure of lipoprotein GNA1162 from neisseria meningitidis

Analyse Crystal structure of lipoprotein GNA1162 from neisseria meningitidis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HRV
Type: protein
Length: 283 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative lipoprotein GNA1162
UniProt: Q7BMM3
Pockets: 3 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative lipoprotein GNA1162	protein	139	40% helix, 29% strand	Q7BMM3
B	Putative lipoprotein GNA1162	protein	144	40% helix, 33% strand	Q7BMM3

Pockets

3 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	94	0.38	0.76	21	empty
2	75	0.33	0.75	16	empty
3	80	0.29	0.72	15	empty

Interfaces

1 interface between chains.

A–B · 2279 Å² buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

4HRV · Crystal Structure of Lipoprotein GNA1162 from Neisseria meningitidis · 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 Q7BMM3
Elsewhere: RCSB PDB 4HRV · PDBe 4HRV · UniProt Q7BMM3

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