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Novel crystal structure of a hypothetical protein from neisseria gonorrhoeae

Analyse Novel crystal structure of a hypothetical protein from neisseria gonorrhoeae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UEB
Type: protein
Length: 286 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NEGOA.19184.A
UniProt: B4RJ46
Ligands: CL
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NEGOA.19184.A	protein	142	15% helix, 43% strand	B4RJ46
B	NEGOA.19184.A	protein	144	15% helix, 43% strand	B4RJ46

Ligands and binding sites

CL · Chloride ion · ion · 3 copies · chains A, B
EDO · 1,2-ethanediol · additive · 11 copies · chains A, B

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

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	187	0.45	0.74	24	EDO

Interfaces

1 interface between chains.

A–B · 351 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5UEB · Novel crystal structure of a hypothetical protein from Neisseria gonorrhoeae · 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 B4RJ46
Elsewhere: RCSB PDB 5UEB · PDBe 5UEB · UniProt B4RJ46

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