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Structure of B. abortus wrba-related protein a (apo)

Analyse Structure of B. abortus wrba-related protein a (apo) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5F51
Type: protein
Length: 165 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NAD(P)H dehydrogenase (quinone)
EC: 1.6.5.2
UniProt: Q2YQ23
Ligands: SO4
Pockets: 2 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NAD(P)H dehydrogenase (quinone) (EC 1.6.5.2)	protein	165	39% helix, 21% strand	Q2YQ23

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

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	56	0.35	0.78	13	empty
2	56	0.28	0.74	19	empty

Compared structures

5F51 · Structure of B. abortus WrbA-related protein A (apo) · the same entry in another collection · chain A against A, TM-score 1.00
Q2YQ23 · AlphaFold monomer V2.0 prediction for NAD(P)H dehydrogenase (quinone) (Q2YQ23) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q2YQ23
Elsewhere: RCSB PDB 5F51 · PDBe 5F51 · UniProt Q2YQ23

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