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Crystal structure of nikz from campylobacter jejuni, unliganded form

Analyse Crystal structure of nikz from campylobacter jejuni, unliganded form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OET
Type: protein
Length: 988 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative peptide ABC-transport system periplasmic peptide- binding protein
UniProt: Q0P844
Pockets: 10 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative peptide ABC-transport system periplasmic peptide- binding protein	protein	494	28% helix, 26% strand	Q0P844

Ligands and binding sites

GOL · Glycerol · additive · 8 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1013	0.88	0.89	119	GOL
2	518	0.82	0.88	72	GOL
3	181	0.80	0.95	40	empty
4	194	0.68	0.86	27	empty
5	282	0.67	0.83	27	empty

Interfaces

1 interface between chains.

A–B · 1145 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

4OET · Crystal structure of NikZ from Campylobacter jejuni, unliganded form · 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 Q0P844
Elsewhere: RCSB PDB 4OET · PDBe 4OET · UniProt Q0P844

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