MolNFT v1 · #93691 · protein

Structure of staphylococcus aureus biotin protein ligase in complex with biotin acetylene

4HA8 · Biotin-[acetyl-CoA-carboxylase] ligase: “Structure of staphylococcus aureus biotin protein ligase in complex with biotin acetylene”. X-ray diffraction, 1 ligand (BC4), 3 pockets (best druggability 0.69). MolNFT v1 #93691 on…

PDB: 4HA8
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: BC4
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Biotin-[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)	protein	322	36% helix, 31% strand	E5R5T0

Ligands and binding sites

BC4 · (3aS,4S,6aR)-4-(hex-5-yn-1-yl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one · 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	304	0.69	0.83	47	BC4
2	75	0.36	0.77	13	empty
3	50	0.31	0.77	14	empty

Compared structures

4HA8 · Structure of Staphylococcus aureus biotin protein ligase in complex with biotin acetylene · 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 4HA8 · PDBe 4HA8 · UniProt E5R5T0

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