Structure of PDB 3mqt Chain U

Receptor sequence

>3mqtU (length=378) Species: 398579 (Shewanella pealeana ATCC 700345) [Search protein sequence]

ANIVSVEFIPVNVASENTVIVKVTDENGVYGLGEADGPPECMKAFSEIEN
EHKWLNNIKEAVIGRDPLEFRANYNRMYDTTKWIGMRGLGLFAISGIDMA
LYDLAGKQLGVPAYKLMGGAQKAQLTPYFTLYPSVAADATLSEIVEAYKP
LIAKAKERGAKAVKVCIIPNDKVSDKEIVAYLRELREVIGWDMDMMVDCL
YRWTDWQKARWTFRQLEDIDLYFIEACLQHDDLIGHQKLAAAINTRLCGA
EMSTTRFEAQEWLEKTGISVVQSDYNRCGGVTELLRIMDICEHHNAQLMP
HNWKTGITAAAARHFGIVCHISEYVEYLHPDFWNGTLTQQLTLNEPKIID
GAIEVSDKPGLGIELNIEFVEQVTGHKF

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)	G37 E40 R87 T130 K154 K164 C166 N170 D198 C199 L200 I224 E225 R246 A250 E251 M252 S269 Q272 D274 H301 N302 E326 D331
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	U	D206 E233 E259	D198 E225 E251

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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