Structure of PDB 1i7c Chain A

Receptor sequence
>1i7cA (length=258) Species: 9606 (Homo sapiens) [Search protein sequence]
cSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNF
MKPSHQGYPHRNFQEEIEFLNAIFPNGAGYCMGRMNSDCWYLYTLDFPES
RVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSV
IDATMFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDL
IRKVVEVFKPGKFVTTLFVNQSTVLASPQKIEGFKRLDCQSAMFNDYNFV
FTSFAKKQ
3D structure
PDB1i7c The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S229 H243
Catalytic site (residue number reindexed from 1) S161 H175
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 PUT A F111 D174 T176 F285 Y318 F44 D107 T109 F218 Y247
BS02 MGB A X68 F223 C226 S229 E247 X1 F156 C159 S162 E180 MOAD: ic50=0.4uM
PDBbind-CN: -logKd/Ki=6.40,IC50=0.4uM
Gene Ontology
Molecular Function
GO:0004014 adenosylmethionine decarboxylase activity
Biological Process
GO:0006597 spermine biosynthetic process
GO:0008295 spermidine biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1i7c, PDBe:1i7c, PDBj:1i7c
PDBsum1i7c
PubMed11583147
UniProtP17707|DCAM_HUMAN S-adenosylmethionine decarboxylase proenzyme (Gene Name=AMD1)

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