Structure of PDB 3no1 Chain A

Receptor sequence
>3no1A (length=355) Species: 312284 (marine actinobacterium PHSC20C1) [Search protein sequence]
LTITRIETIPMVAPLAHRATIVTRVHTDAGIIGEAYTGDEHETMFDIDRI
IHEELAPTLIGQDAMAIERLWDSGYKVTFDILRDRRLGLVALAAVNTAIW
DAVGKALKMPLWKLWGGYRNELPMIAIGGYYGEPLGSIADEMHNYQELGL
AGVKFKVGGLSAAEDAARITAAREAAGDDFIICIDANQGYKPAVAVDLSR
RIADLNIRWFEEPVEWHNDKRSMRDVRYQGSVPVCAGQTEFSASGCRDLM
ETGAIDVCNFDSSWSGGPTAWLRTAAIATSYDVQMGHHEEPQVSTHLLAS
QPHGTIAECFHPDRDPFWWNMITNRPKLNNGTLTLSDRPGLGWDLNWDYI
DQYRV
3D structure
PDB3no1 Crystal Structure of Mandelate racemase/muconate lactonizing enzyme from a Marine actinobacterium in complex with magnesium
ChainA
Resolution2.16 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D69 I157 K184 K186 I214 D215 A216 N217 E241 G267 Q268 N289 D291 H318 E319 E320 E338 D343
Catalytic site (residue number reindexed from 1) D39 I127 K154 K156 I184 D185 A186 N187 E211 G237 Q238 N259 D261 H288 E289 E290 E308 D313
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 A D215 E241 Q268 D185 E211 Q238
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3no1, PDBe:3no1, PDBj:3no1
PDBsum3no1
PubMed
UniProtA4AFX2

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