Structure of PDB 3cbg Chain A

Receptor sequence
>3cbgA (length=218) Species: 1148 (Synechocystis sp. PCC 6803) [Search protein sequence]
KGITGFDPSLYSYLQSISADDSFYLAQLRRETAHLPGAPMQISPEQAQFL
GLLISLTGAKQVLEIGVFRGYSALAMALQLPPDGQIIACDQDPNATAIAK
KYWQKAGVAEKISLRLGPALATLEQLTQGKPLPEFDLIFIDADKRNYPRY
YEIGLNLLRRGGLMVIDNVLWHGKVTEVDPQEAQTQVLQQFNRDLAQDER
VRISVIPLGDGMTLALKK
3D structure
PDB3cbg Functional and Structural Characterization of a Cation-dependent O-Methyltransferase from the Cyanobacterium Synechocystis sp. Strain PCC 6803
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D143 K146 D169 N170
Catalytic site (residue number reindexed from 1) D141 K144 D167 N168
Enzyme Commision number 2.1.1.-
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 MG A D143 D169 N170 D141 D167 N168
BS02 SAH A M42 Q43 I44 G68 V69 F70 S74 D92 Q93 P120 A121 D143 A144 D145 M40 Q41 I42 G66 V67 F68 S72 D90 Q91 P118 A119 D141 A142 D143
BS03 FER A M42 K146 N170 H174 M40 K144 N168 H172
BS04 4FE A M42 D143 K146 N170 W173 H174 M40 D141 K144 N168 W171 H172
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008171 O-methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:3cbg, PDBe:3cbg, PDBj:3cbg
PDBsum3cbg
PubMed18502765
UniProtQ55813

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