Structure of PDB 3c6k Chain D

Receptor sequence
>3c6kD (length=348) Species: 9606 (Homo sapiens) [Search protein sequence]
GSRHSTLDFMLDGETILKGLQSIFQEQGMAESVHTWQDHGYLATYTNKNG
SFANLRIYPHGLVLLDLQSYDGDAQGKEEIDSILNKVEERMKELGRVKRL
PPIVRGGAIDRYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNI
LILSGDVNLAESDLAYTRAIMGSGKEDYTGKDVLILGGGDGGILCEIVKL
KPKMVTMVEIDQMVIDGCKKYMRKDVLDNLKGDCYQVLIEDCIPVLKRYA
KEGREFDYVINDLTAVPISTSPSTWEFLRLILDLSMKVLKQDGKYFTQGN
CVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTVWKKAK
3D structure
PDB3c6k Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism.
ChainD
Resolution1.95 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.5.1.22: spermine synthase.
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 SPD D D169 V170 N171 L279 Y353 E355 W357 D156 V157 N158 L263 Y334 E336 W338
BS02 MTA D L166 N171 G200 G201 G202 E222 I223 C258 D278 L279 T280 I284 L153 N158 G187 G188 G189 E209 I210 C242 D262 L263 T264 I268 MOAD: Ki=0.3uM
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0016768 spermine synthase activity
Biological Process
GO:0006555 methionine metabolic process
GO:0006595 polyamine metabolic process
GO:0006596 polyamine biosynthetic process
GO:0006597 spermine biosynthetic process
GO:0008215 spermine metabolic process
Cellular Component
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3c6k, PDBe:3c6k, PDBj:3c6k
PDBsum3c6k
PubMed18367445
UniProtP52788|SPSY_HUMAN Spermine synthase (Gene Name=SMS)

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