Structure of PDB 3h0v Chain A

Receptor sequence
>3h0vA (length=239) Species: 9606 (Homo sapiens) [Search protein sequence]
SMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFM
KPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPDQT
LEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPC
GYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFK
PGKFVTTLFVNQKIEGFKRLDCQSAMFNDYNFVFTSFAK
3D structure
PDB3h0v Role of the sulfonium center in determining the ligand specificity of human s-adenosylmethionine decarboxylase.
ChainA
Resolution2.24 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) S229 H243
Catalytic site (residue number reindexed from 1) S153 H167
Enzyme Commision number 4.1.1.50: adenosylmethionine 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 M2T A F223 C226 G227 Y228 S229 I244 T245 E247 F147 C150 G151 Y152 S153 I168 T169 E171 MOAD: ic50=15uM
PDBbind-CN: -logKd/Ki=4.82,IC50=15uM
BS02 PYR A S69 K80 T81 H243 S1 K12 T13 H167
Gene Ontology
Molecular Function
GO:0004014 adenosylmethionine decarboxylase activity
Biological Process
GO:0006597 spermine biosynthetic process
GO:0008295 spermidine biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3h0v, PDBe:3h0v, PDBj:3h0v
PDBsum3h0v
PubMed19527050
UniProtP17707|DCAM_HUMAN S-adenosylmethionine decarboxylase proenzyme (Gene Name=AMD1)

[Back to BioLiP]