Structure of PDB 1i7m Chain C

Receptor sequence
>1i7mC (length=249) Species: 9606 (Homo sapiens) [Search protein sequence]
cSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNF
MKPSHQGYPHRNFQEEIEFLNAIFPNGAGYCMGRMNSDCWYLYTLDFQPD
QTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFN
PCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEV
FKPGKFVTTLFVNQSSKCPQKIEGFKRLDCQSAMFNDYNFVFTSFAKKQ
3D structure
PDB1i7m The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase.
ChainC
Resolution2.24 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S1229 H1243
Catalytic site (residue number reindexed from 1) S154 H168
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 C F1111 T1176 F1285 Y1318 F44 T102 F211 Y238
BS02 CG C X1068 C1082 F1223 C1226 S1229 I1244 T1245 E1247 X1 C15 F149 C152 S155 I170 T171 E173
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:1i7m, PDBe:1i7m, PDBj:1i7m
PDBsum1i7m
PubMed11583147
UniProtP17707|DCAM_HUMAN S-adenosylmethionine decarboxylase proenzyme (Gene Name=AMD1)

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