Structure of PDB 2gn2 Chain A

Receptor sequence

>2gn2A (length=326)

ITYDLPVAIEDILEAKKRLAGKIYKTGMPRSNYFSERCKGEIFLKFENMQ
RTGSFKIRGAFNKLSSLTEAEKRKGVVACSAGNHAQGVSLSCAMLGIDGK
VVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVETEGRIFIPP
YDDPKVIAGQGTIGLEIMEDLYDVDNVIVPIGGGGLIAGIAIAIKSINPT
IKVIGVQAENVHGMAASYYTGEITTHRTTGTLADGCDVSRPGNLTYEIVR
ELVDDIVLVSEDEIRNSMIALIQRNKVITEGAGALACAALLSGKLDSHIQ
NRKTVSIISGGNIDLSRVSQITGLVD

3D structure

• PDB: 2gn2 Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex with CMP provide structural insights into ligand-induced oligomerization and enzyme activation.
• Chain: A
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K58 A83 Q209 V213 G215 G237 I310 S311
• Catalytic site (residue number reindexed from 1): K56 A81 Q207 V211 G213 G235 I308 S309
• Enzyme Commision number: 4.3.1.17: L-serine ammonia-lyase.
  4.3.1.19: threonine ammonia-lyase.

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	C5P	A	R53 T54 G55 A116 D119 Y120 N314	R51 T52 G53 A114 D117 Y118 N312

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0003941 L-serine ammonia-lyase activity
• GO:0004794 threonine deaminase activity
• GO:0016829 lyase activity
• GO:0030170 pyridoxal phosphate binding

Biological Process

• GO:0006520 amino acid metabolic process
• GO:0006565 L-serine catabolic process
• GO:0006567 threonine catabolic process
• GO:0009097 isoleucine biosynthetic process
• GO:0070689 L-threonine catabolic process to propionate

External links

• PDB: RCSB:2gn2, PDBe:2gn2, PDBj:2gn2
• PDBsum: 2gn2
• PubMed: 17046821
• UniProt: P11954|TDCB_SALTY L-threonine dehydratase catabolic TdcB (Gene Name=tdcB)