Structure of PDB 1m0n Chain A

Receptor sequence
>1m0nA (length=431) Species: 292 (Burkholderia cepacia) [Search protein sequence]
LNDDATFWRNARHHLVRYGGTFEPMIIERAKGSFVYDADGRAILDFTSGQ
MSAVLGHCHPEIVSVIGEYAGKLDHLFSEMLSRPVVDLATRLANITPPGL
DRALLLSTGAESNEAAIRMAKLVTGKYEIVGFAQSWHGMTGAAASATYSA
GRKGVGPAAVGSFAIPAPFTYRPRFERNGAYDYLAELDYAFDLIDRQSSG
NLAAFIAEPILSSGGIIELPDGYMAALKRKCEARGMLLILDEAQTGVGRT
GTMFACQRDGVTPDILTLSKTLGAGLPLAAIVTSAAIEERAHELGYLFYT
THVSDPLPAAVGLRVLDVVQRDGLVARANVMGDRLRRGLLDLMERFDCIG
DVRGRGLLLGVEIVKDRRTKEPADGLGAKITRECMNLGLSMNIVQLPGMG
GVFRIAPPLTVSEDEIDLGLSLLGQAIERAL
3D structure
PDB1m0n Aminophosphonate Inhibitors of Dialkylglycine Decarboxylase: Structural Basis for Slow Binding Inhibition
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G21 W138 E210 D243 Q246 K272 T303 R406
Catalytic site (residue number reindexed from 1) G19 W136 E208 D241 Q244 K270 T301 R404
Enzyme Commision number 4.1.1.64: 2,2-dialkylglycine decarboxylase (pyruvate).
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 HCP A Q52 M53 A112 N115 W138 H139 E210 S215 D243 A245 Q246 K272 R406 Q50 M51 A110 N113 W136 H137 E208 S213 D241 A243 Q244 K270 R404 MOAD: Ki=6mM
PDBbind-CN: -logKd/Ki=2.22,Ki=6.0mM
Gene Ontology
Molecular Function
GO:0008453 alanine-glyoxylate transaminase activity
GO:0008483 transaminase activity
GO:0016831 carboxy-lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0047432 2,2-dialkylglycine decarboxylase (pyruvate) activity
Biological Process
GO:0009436 glyoxylate catabolic process
GO:0019481 L-alanine catabolic process, by transamination

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Molecular Function
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Biological Process
External links
PDB RCSB:1m0n, PDBe:1m0n, PDBj:1m0n
PDBsum1m0n
PubMed12369820
UniProtP16932|DGDA_BURCE 2,2-dialkylglycine decarboxylase (Gene Name=dgdA)

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