Structure of PDB 1lkc Chain A

Receptor sequence
>1lkcA (length=355) Species: 28901 (Salmonella enterica) [Search protein sequence]
HGGNIREPATVLGISPDQLLDFSANINPLGMPVSVKRALIDNLDCIERYP
DADYFHLHQALARHHQVPASWILAGNGETESIFTVASGLKPRRAMIVTPG
FAEYGRALAQSGCEIRRWSLREADGWQLTDAILEALTPDLDCLFLCTPNN
PTGLLPERPLLQAIADRCKSLNINLILDEAFIDFIPHETGFIPALKDNPH
IWVLRSLTKFYAIPGLRLGYLVNSDDAAMARMRRQQMPWSVNALAALAGE
VALQDSAWQQATWHWLREEGARFYQALCQLPLLTVYPGRANYLLLRCERE
DIDLQRRLLTQRILIRSCANYPGLDSRYYRVAIRSAAQNERLLAALRNVL
TGIAP
3D structure
PDB1lkc Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica.
ChainA
Resolution1.8 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 H1 G2 N150 R316 R330
BS02 PLP A G84 E85 T86 F108 D185 A187 F188 S213 T215 K216 R224 G77 E78 T79 F101 D178 A180 F181 S206 T208 K209 R217
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:1lkc, PDBe:1lkc, PDBj:1lkc
PDBsum1lkc
PubMed11939774
UniProtP97084|COBD_SALTY Threonine-phosphate decarboxylase (Gene Name=cobD)

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