Structure of PDB 4eml Chain F

Receptor sequence
>4emlF (length=259) Species: 1111708 (Synechocystis sp. PCC 6803 substr. Kazusa) [Search protein sequence]
MDWHIAKHYDDILYYKAGGIAKIVINRPHKRNAFRPQTVFELYDAFCNAR
EDNRIGVVLLTGAGPHSDGKYAFCSGGDQLNVLDLQRLIRSMPKVVIALV
AGYAIGGGHVLHLVCDLTIAADNAIFGQTGPKVGSFDGGFGSSYLARIVG
QKKAREIWYLCRQYSAQEAERMGMVNTVVPVDRLEEEGIQWAKEILSKSP
LAIRCLKAAFNADCDGQAGLQELAGNATLLYYMTEEGSEGKQAFLEKRPP
DFSQYPWLP
3D structure
PDB4eml Active site binding and catalytic role of bicarbonate in 1,4-dihydroxy-2-naphthoyl coenzyme A synthases from vitamin K biosynthetic pathways
ChainF
Resolution2.043 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) G77 L99 G123 V126 G146 S151 D153 G154 A240 Y248
Catalytic site (residue number reindexed from 1) G77 L83 G107 V110 G130 S135 D137 G138 A224 Y232
Enzyme Commision number 4.1.3.36: 1,4-dihydroxy-2-naphthoyl-CoA 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 BCT F G122 Q144 G146 W174 G106 Q128 G130 W158
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008935 1,4-dihydroxy-2-naphthoyl-CoA synthase activity
GO:0016829 lyase activity
Biological Process
GO:0009234 menaquinone biosynthetic process
GO:0042372 phylloquinone biosynthetic process
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4eml, PDBe:4eml, PDBj:4eml
PDBsum4eml
PubMed22606952
UniProtP73495

[Back to BioLiP]