Structure of PDB 3dg7 Chain A

Receptor sequence

>3dg7A (length=366) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]

MKIVAIGAIPFSIPYTKPLRFASGEVHAAEHVLVRVHTDDGIVGVAEAPP
RPFTYGETQTGIVAVIEQYFAPALIGLTLTEREVAHTRMARTVGNPTAKA
AIDMAMWDALGQSLRLSVSEMLGGYTDRMRVSHMLGFDDPVKMVAEAERI
RETYGINTFKVKVGRRPVQLDTAVVRALRERFGDAIELYVDGNRGWSAAE
SLRAMREMADLDLLFAEELCPADDVLSRRRLVGQLDMPFIADESVPTPAD
VTREVLGGSATAISIKTARTGFTGSTRVHHLAEGLGLDMVMGNQIDGQIG
TACTVSFGTAFERTSRHAGELSNFLDMSDDLLTVPLQISDGQLHRRPGPG
LGIEIDPDKLAHYRTD

3D structure

PDB

3dg7 Evolution of enzymatic activities in the enolase superfamily: stereochemically distinct mechanisms in two families of cis,cis-muconate lactonizing enzymes

Chain

Resolution

2.0 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	L19 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)	L19 P50 R51 M134 K160 K162 D191 N193 E217 D242 E243 S244 K266 G292 N293 Q294 G319 E320 L321
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	D191 E217 D242
BS02	MUC	A	F21 M134 K160 K162 D191 N193 D242 K266 N293 Q294	F21 M134 K160 K162 D191 N193 D242 K266 N293 Q294

Gene Ontology

	Molecular Function
GO:0003824	catalytic activity
GO:0046872	metal ion binding

	Biological Process
GO:0009234	menaquinone biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:3dg7, PDBe:3dg7, PDBj:3dg7
PDBsum	3dg7
PubMed	19220063
UniProt	A0QTN8

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