Structure of PDB 2d3m Chain A

Receptor sequence
>2d3mA (length=405) Species: 45385 (Aloe arborescens) [Search protein sequence]
GPGMSSLSNSLPLMEDVQGIRKAQKADGTATVMAIGTAHPPHIFPQDTYA
DVYFRATNSEHKVELKKKFDHICKKTMIGKRYFNYDEEFLKKYPNITSYD
EPSLNDRQDICVPGVPALGTEAAVKAIEEWGRPKSEITHLVFCTSCGVDM
PSADFQCAKLLGLHANVNKYCIYMQGCYAGGTVMRYAKDLAENNRGARVL
VVCAELTIMMLRAPNETHLDNAIGISLFGDGAAALIIGSDPIIGVEKPMF
EIVCTKQTVIPNTEDVIHLHLRETGMMFYLSKGSPMTISNNVEACLIDVF
KSVGITPPEDWNSLFWIPHPGGRAILDQVEAKLKLRPEKFRAARTVLWDY
GNMVSASVGYILDEMRRKSAAKGLETYGEGLEWGVLLGFGPGITVETILL
HSLPL
3D structure
PDB2d3m Structural Insight into Chain-Length Control and Product Specificity of Pentaketide Chromone Synthase from Aloe arborescens
ChainA
Resolution1.6 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) C177 F228 H319 N352
Catalytic site (residue number reindexed from 1) C177 F228 H319 N352
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 A H71 K75 A177 I223 L227 F278 L280 S281 G321 G322 R323 A324 I325 H71 K75 A177 I223 L227 F278 L280 S281 G321 G322 R323 A324 I325
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

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

[Back to BioLiP]