Structure of PDB 2d3m Chain B

Receptor sequence
>2d3mB (length=395) Species: 45385 (Aloe arborescens) [Search protein sequence]
LPLMEDVQGIRKAQKADGTATVMAIGTAHPPHIFPQDTYADVYFRATNSE
HKVELKKKFDHICKKTMIGKRYFNYDEEFLKKYPNITSYDEPSLNDRQDI
CVPGVPALGTEAAVKAIEEWGRPKSEITHLVFCTSCGVDMPSADFQCAKL
LGLHANVNKYCIYMQGCYAGGTVMRYAKDLAENNRGARVLVVCAELTIMM
LRAPNETHLDNAIGISLFGDGAAALIIGSDPIIGVEKPMFEIVCTKQTVI
PNTEDVIHLHLRETGMMFYLSKGSPMTISNNVEACLIDVFKSVGITPPED
WNSLFWIPHPGGRAILDQVEAKLKLRPEKFRAARTVLWDYGNMVSASVGY
ILDEMRRKSAAKGLETYGEGLEWGVLLGFGPGITVETILLHSLPL
3D structure
PDB2d3m Structural Insight into Chain-Length Control and Product Specificity of Pentaketide Chromone Synthase from Aloe arborescens
ChainB
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C177 F228 H319 N352
Catalytic site (residue number reindexed from 1) C167 F218 H309 N342
Enzyme Commision number 2.3.1.216: 5,7-dihydroxy-2-methylchromone 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 COA B K68 A177 I223 F228 F278 L280 K282 G321 G322 R323 A324 I325 K58 A167 I213 F218 F268 L270 K272 G311 G312 R313 A314 I315
Gene Ontology
Molecular Function
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0042803 protein homodimerization activity
Biological Process
GO:0009058 biosynthetic process
GO:0009813 flavonoid biosynthetic process
GO:0030639 polyketide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2d3m, PDBe:2d3m, PDBj:2d3m
PDBsum2d3m
PubMed17462571
UniProtQ58VP7|PCS_ALOAR 5,7-dihydroxy-2-methylchromone synthase

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