Structure of PDB 1lc8 Chain A

Receptor sequence
>1lc8A (length=356) Species: 28901 (Salmonella enterica) [Search protein sequence]
AHGGNIREPATVLGISPDQLLDFSANINPLGMPVSVKRALIDNLDCIERY
PDADYFHLHQALARHHQVPASWILAGNGETESIFTVASGLKPRRAMIVTP
GFAEYGRALAQSGCEIRRWSLREADGWQLTDAILEALTPDLDCLFLCTPN
NPTGLLPERPLLQAIADRCKSLNINLILDEAFIDFIPHETGFIPALKDNP
HIWVLRSLTKFYAIPGLRLGYLVNSDDAAMARMRRQQMPWSVNALAALAG
EVALQDSAWQQATWHWLREEGARFYQALCQLPLLTVYPGRANYLLLRCER
EDIDLQRRLLTQRILIRSCANYPGLDSRYYRVAIRSAAQNERLLAALRNV
LTGIAP
3D structure
PDB1lc8 Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: the apo, substrate, and product-aldimine complexes.
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 33P A H8 G9 G84 E85 T86 F108 N157 D185 A187 S213 T215 K216 R224 R323 R337 H2 G3 G78 E79 T80 F102 N151 D179 A181 S207 T209 K210 R218 R317 R331
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:1lc8, PDBe:1lc8, PDBj:1lc8
PDBsum1lc8
PubMed12119022
UniProtP97084|COBD_SALTY Threonine-phosphate decarboxylase (Gene Name=cobD)

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