Structure of PDB 1bs1 Chain A

Receptor sequence

>1bs1A (length=224) Species: 562 (Escherichia coli)

SKRYFVTGTDTEVGKTVASCALLQAAKAAGYRTAGYKPVASGSEKTPEGL
RNSDALALQRNSSLQLDYATVNPYTFAEPTSPHIISAQEGRPIESLVMSA
GLRALEQQADWVLVEGAGGWFTPLSDTFTFADWVTQEQLPVILVVGVKLG
CINHAMLTAQVIQHAGLTLAGWVANDVTPPGKRHAEYMTTLTRMIPAPLL
GEIPWLAENPENAATGKYINLALL

3D structure

• PDB: 1bs1 Crystal structure of two quaternary complexes of dethiobiotin synthetase, enzyme-MgADP-AlF3-diaminopelargonic acid and enzyme-MgADP-dethiobiotin-phosphate; implications for catalysis.
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T11 E12 K15 T16 K37 S41 D54 E115
• Catalytic site (residue number reindexed from 1): T11 E12 K15 T16 K37 S41 D54 E115
• Enzyme Commision number: 6.3.3.3: dethiobiotin synthase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	MG	A	T16 D54 E115	T16 D54 E115
BS02	ADP	A	E12 G14 K15 T16 V17 N175 D176 W205 L206 P210 E211	E12 G14 K15 T16 V17 N175 D176 W205 L206 P210 E211
BS03	DAA	A	T11 K15 K37 S41 D54 P79 A117 G118	T11 K15 K37 S41 D54 P79 A117 G118

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004141 dethiobiotin synthase activity
• GO:0005524 ATP binding
• GO:0016874 ligase activity
• GO:0042803 protein homodimerization activity
• GO:0046872 metal ion binding

Biological Process

• GO:0009102 biotin biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1bs1, PDBe:1bs1, PDBj:1bs1
• PDBsum: 1bs1
• PubMed: 9865950
• UniProt: P13000|BIOD1_ECOLI ATP-dependent dethiobiotin synthetase BioD 1 (Gene Name=bioD1)