Structure of PDB 1i79 Chain A

Receptor sequence
>1i79A (length=252) Species: 9606 (Homo sapiens) [Search protein sequence]
cSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNF
MKPSHQGYPHRNFQEEIEFLNAIFPNGAGYCMGRMNSDCWYLYTLDFPES
QPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDAT
MFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKV
VEVFKPGKFVTTLFVNQSSKCRPQKIEGFKRLDCQSAMFNDYNFVFTSFA
KK
3D structure
PDB1i79 The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase.
ChainA
Resolution2.01 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) 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 MHZ A X68 C82 F223 C226 G227 Y228 S229 I244 T245 E247 X1 C15 F152 C155 G156 Y157 S158 I173 T174 E176
BS02 PUT A F111 D174 T176 F285 Y318 F44 D103 T105 F214 Y242
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:1i79, PDBe:1i79, PDBj:1i79
PDBsum1i79
PubMed11583147
UniProtP17707|DCAM_HUMAN S-adenosylmethionine decarboxylase proenzyme (Gene Name=AMD1)

[Back to BioLiP]