Structure of PDB 1lc5 Chain A

Receptor sequence
>1lc5A (length=355) Species: 28901 (Salmonella enterica) [Search protein sequence]
LFNTAHGGNIREPATVLGISPDQLLDFSANINPLGMPVSVKRALIDNLDC
IERYPDADYFHLHQALARHHQVPASWILAGNGETESIFTVASGLKPRRAM
IVTPGFAEYGRALAQSGCEIRRWSLREADGWQLTDAILEALTPDLDCLFL
CTPNNPTGLLPERPLLQAIADRCKSLNINLILDEAFIDFIPHETGFIPAL
KDNPHIWVLRSLTKFYAIPGLRLGYLVNSDDAAMARMRRQQMPWSVNALA
ALAGEVALQDSAWQQATWHWLREEGARFYQALCQLPLLTVYPGRANYLLL
RCEREDIDLQRRLLTQRILIRSCANYPGLDSRYYRVAIRSAAQNERLLAA
LRNVL
3D structure
PDB1lc5 Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: the apo, substrate, and product-aldimine complexes.
ChainA
Resolution1.46 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.81: threonine-phosphate decarboxylase.
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 PO4 A H8 G9 N157 R323 R337 H6 G7 N155 R321 R335
BS02 PO4 A G84 E85 T86 S213 T215 K216 R224 G82 E83 T84 S211 T213 K214 R222
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0048472 threonine-phosphate decarboxylase activity
Biological Process
GO:0009058 biosynthetic process
GO:0009236 cobalamin biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1lc5, PDBe:1lc5, PDBj:1lc5
PDBsum1lc5
PubMed12119022
UniProtP97084|COBD_SALTY Threonine-phosphate decarboxylase (Gene Name=cobD)

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