Structure of PDB 3mqt Chain G

Receptor sequence

>3mqtG (length=377) Species: 398579 (Shewanella pealeana ATCC 700345) [Search protein sequence]

ANIVSVEFIPVNVAENTVIVKVTDENGVYGLGEADGPPECMKAFSEIENE
HKWLNNIKEAVIGRDPLEFRANYNRMYDTTKWIGMRGLGLFAISGIDMAL
YDLAGKQLGVPAYKLMGGAQKAQLTPYFTLYPSVAADATLSEIVEAYKPL
IAKAKERGAKAVKVCIIPNDKVSDKEIVAYLRELREVIGWDMDMMVDCLY
RWTDWQKARWTFRQLEDIDLYFIEACLQHDDLIGHQKLAAAINTRLCGAE
MSTTRFEAQEWLEKTGISVVQSDYNRCGGVTELLRIMDICEHHNAQLMPH
NWKTGITAAAARHFGIVCHISEYVEYLHPDFWNGTLTQQLTLNEPKIIDG
AIEVSDKPGLGIELNIEFVEQVTGHKF

3D structure

PDB

3mqt Crystal STRUCTURE OF A MANDELATE RACEMASE/MUCONATE LACTONIZING ENZYME FROM SHEWANELLA PEALEANA

Chain

Resolution

2.1 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	G45 E48 R95 T138 K162 K172 C174 N178 D206 C207 L208 I232 E233 R254 A258 E259 M260 S277 Q280 D282 H309 N310 E334 D339
Catalytic site (residue number reindexed from 1)	G36 E39 R86 T129 K153 K163 C165 N169 D197 C198 L199 I223 E224 R245 A249 E250 M251 S268 Q271 D273 H300 N301 E325 D330
Enzyme Commision number	?

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	G	D206 E233 E259	D197 E224 E250

Gene Ontology

	Molecular Function
GO:0000287	magnesium ion binding
GO:0016836	hydro-lyase activity
GO:0046872	metal ion binding

	Biological Process
GO:0016052	carbohydrate catabolic process

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:3mqt, PDBe:3mqt, PDBj:3mqt
PDBsum	3mqt
PubMed
UniProt	A8H7M5

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