Structure of PDB 3mle Chain F

Receptor sequence
>3mleF (length=223) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence]
FQGHMLFISATNTNAGKTTCARLLAQYCNACGVKTILLKPIETGVNDAIN
HSSDAHLFLQDNRLLDRSLTLKDISFYRYHKVSAPLIAQQEEDPNAPIDT
DNLTQRLHNFTKTYDLVIVEGAGGLCVPITLEENMLDFALKLKAKMLLIS
HDNLGLINDCLLNDFLLKSHQLDYKIAINLKGNNTAFHSISLPYIELFNT
RSNNPIVIFQQSLKVLMSFALKG
3D structure
PDB3mle Structural characterization of Helicobacter pylori dethiobiotin synthetase reveals differences between family members.
ChainF
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T9 N10 K13 T14 K35 T39 D50 E116
Catalytic site (residue number reindexed from 1) T13 N14 K17 T18 K39 T43 D54 E120
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 8AC F T39 G119 V123 T43 G123 V127
BS02 MG F T14 D50 E116 T18 D54 E120
BS03 8AC F L150 G151 I153 L154 G155 I157
BS04 ADP F N10 A11 G12 K13 T14 T15 N175 K177 N14 A15 G16 K17 T18 T19 N179 K181
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004141 dethiobiotin synthase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0009102 biotin biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3mle, PDBe:3mle, PDBj:3mle
PDBsum3mle
PubMed22284390
UniProtO24872|BIOD_HELPY ATP-dependent dethiobiotin synthetase BioD (Gene Name=bioD)

[Back to BioLiP]