Structure of PDB 3mle Chain A

Receptor sequence
>3mleA (length=221) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence]
GHMLFISATNTNAGKTTCARLLAQYCNACGVKTILLKPIETGVNDAINHS
SDAHLFLQDNRLLDRSLTLKDISFYRYHKVSAPLIAQQEEDPNAPIDTDN
LTQRLHNFTKTYDLVIVEGAGGLCVPITLEENMLDFALKLKAKMLLISHD
NLGLINDCLLNDFLLKSHQLDYKIAINLKGNNTAFHSISLPYIELFNTRS
NNPIVIFQQSLKVLMSFALKG
3D structure
PDB3mle Structural characterization of Helicobacter pylori dethiobiotin synthetase reveals differences between family members.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T9 N10 K13 T14 K35 T39 D50 E116
Catalytic site (residue number reindexed from 1) T11 N12 K15 T16 K37 T41 D52 E118
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 T14 D50 E116 T16 D52 E118
BS02 8AC A G151 I153 N154 G153 I155 N156
BS03 ADP A N10 A11 G12 K13 T14 T15 N175 N12 A13 G14 K15 T16 T17 N177 PDBbind-CN: -logKd/Ki=5.24,Kd=5.8uM
BS04 8AC A T39 S79 A80 V123 T41 S81 A82 V125
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

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Molecular Function

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Biological Process

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

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