Structure of PDB 1i7b Chain A

Receptor sequence
>1i7bA (length=251) Species: 9606 (Homo sapiens) [Search protein sequence]
cSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNF
MKPSHQGYPHRNFQEEIEFLNAIFPNGAGYCMGRMNSDCWYLYTLDFPES
QPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDAT
MFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKV
VEVFKPGKFVTTLFVNQSSKCPQKIEGFKRLDCQSAMFNDYNFVFTSFAK
K
3D structure
PDB1i7b The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase.
ChainA
Resolution1.9 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) S157 H171
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 SMM A X68 T81 C82 F223 N224 C226 G227 Y228 S229 I244 T245 E247 X1 T14 C15 F152 N153 C155 G156 Y157 S158 I173 T174 E176
BS02 PUT A F111 T176 F285 F44 T105 F214
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
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Biological Process
External links
PDB RCSB:1i7b, PDBe:1i7b, PDBj:1i7b
PDBsum1i7b
PubMed11583147
UniProtP17707|DCAM_HUMAN S-adenosylmethionine decarboxylase proenzyme (Gene Name=AMD1)

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