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Structure of the nucleotide binding domain of an ABC transporter msba from acinetobacter baumannii

Analyse Structure of the nucleotide binding domain of an ABC transporter msba from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5IDV
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipid a export ATP-BINDING/PERMEASE protein msba
EC: 3.6.3.-
UniProt: A0A0Q2LVW2
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipid a export ATP-BINDING/PERMEASE protein msba (EC 3.6.3.-)	protein	263	36% helix, 24% strand	A0A0Q2LVW2

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	246	0.53	0.76	30	empty
2	63	0.48	0.84	16	EDO

Compared structures

5IDV · Structure of the nucleotide binding domain of an ABC transporter MsbA from Acinetobacter… · 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 A0A0Q2LVW2
Elsewhere: RCSB PDB 5IDV · PDBe 5IDV · UniProt A0A0Q2LVW2

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