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Structure of staphylococcus aureus biotin protein ligase in complex with biotinol-5'-AMP

Analyse Structure of staphylococcus aureus biotin protein ligase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DQ2
Type: protein
Length: 322 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Biotin-[acetyl-CoA-carboxylase] ligase
EC: 6.3.4.15
UniProt: E5R5T0
Ligands: BTX
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Biotin-[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)	protein	322	35% helix, 31% strand	E5R5T0

Ligands and binding sites

BTX · ((2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxy-tetrahydrofuran-2-yl)methyl 5-((3as,4s,6ar)-2-oxo-hexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentyl hydrogen phosphate · ligand · chains A

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

Pockets

3 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	284	0.71	0.85	48	BTX
2	86	0.41	0.78	13	empty
3	56	0.33	0.77	12	empty

Compared structures

4DQ2 · Structure of staphylococcus aureus biotin protein ligase in complex with biotinol-5'-amp · 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 E5R5T0
Elsewhere: RCSB PDB 4DQ2 · PDBe 4DQ2 · UniProt E5R5T0

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