Structure of PDB 3dg3 Chain A

Receptor sequence
>3dg3A (length=355) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
MKIVAIGAIPFSIPYTAAEHVLVRVHTDDGIVGVAEAPPRPFTYGETQTG
IVAVIEQYFAPALIGLTLTEREVAHTRMARTVGNPTAKAAIDMAMWDALG
QSLRLSVSEMLGGYTDRMRVSHMLGFDDPVKMVAEAERIRETYGINTFKV
KVGRRPVQLDTAVVRALRERFGDAIELYVDGNRGWSAAESLRAMREMADL
DLLFAEELCPADDVLSRRRLVGQLDMPFIADESVPTPADVTREVLGGSAT
AISIKTARTGFTGSTRVHHLAEGLGLDMVMGNQIDGQIGTACTVSFGTAF
ERTSRHAGELSNFLDMSDDLLTVPLQISDGQLHRRPGPGLGIEIDPDKLA
HYRTD
3D structure
PDB3dg3 Evolution of enzymatic activities in the enolase superfamily: stereochemically distinct mechanisms in two families of cis,cis-muconate lactonizing enzymes
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) P50 R51 M134 K160 K162 D191 N193 E217 D242 E243 S244 K266 G292 N293 Q294 G319 E320 L321
Catalytic site (residue number reindexed from 1) P39 R40 M123 K149 K151 D180 N182 E206 D231 E232 S233 K255 G281 N282 Q283 G308 E309 L310
Enzyme Commision number 5.5.1.-
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 D191 E217 D242 D180 E206 D231
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0046872 metal ion binding
Biological Process
GO:0009234 menaquinone biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3dg3, PDBe:3dg3, PDBj:3dg3
PDBsum3dg3
PubMed19220063
UniProtA0QTN8

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