Structure of PDB 4i52 Chain A

Receptor sequence
>4i52A (length=275) Species: 1111708 (Synechocystis sp. PCC 6803 substr. Kazusa) [Search protein sequence]
MDWHIAKHYDDILYYKAGGIAKIVINRPHKRNAFRPQTVFELYDAFCNAR
EDNRIGVVLLTGAGPHSDGKYAFCSGGDQSVRGEGGYIDDQGTPRLNVLD
LQRLIRSMPKVVIALVAGYAIGGGHVLHLVCDLTIAADNAIFGQTGPKVG
SFDGGFGSSYLARIVGQKKAREIWYLCRQYSAQEAERMGMVNTVVPVDRL
EEEGIQWAKEILSKSPLAIRCLKAAFNADCDGQAGLQELAGNATLLYYMT
EEGSEGKQAFLEKRPPDFSQYPWLP
3D structure
PDB4i52 Structural basis of the induced-fit mechanism of 1,4-dihydroxy-2-naphthoyl coenzyme a synthase from the crotonase fold superfamily
ChainA
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G77 R82 Y87 R95 L99 G123 V126 G146 S151 D153 G154 A240 Y248
Catalytic site (residue number reindexed from 1) G77 R82 Y87 R95 L99 G123 V126 G146 S151 D153 G154 A240 Y248
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 1HA A H29 K30 R31 A33 S75 G76 G77 D78 Q79 L96 V98 Y119 I121 G123 T145 V149 S151 F152 H29 K30 R31 A33 S75 G76 G77 D78 Q79 L96 V98 Y119 I121 G123 T145 V149 S151 F152
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

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Cellular Component
External links
PDB RCSB:4i52, PDBe:4i52, PDBj:4i52
PDBsum4i52
PubMed23658663
UniProtP73495

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