Structure of PDB 2qa2 Chain A

Receptor sequence

>2qa2A (length=489) Species: 1883 (Streptomyces)

SDASVIVVGAGPAGLMLAGELRLGGVDVMVLEQLPQRTGESRGLGFTART
MEVFDQRGILPAFGPVETSTQGHFGGRPVDFGVLEGAHYGVKAVPQSTTE
SVLEEWALGRGAELLRGHTVRALTDEGDHVVVEVEGPDGPRSLTTRYVVG
CDGGRSTVRKAAGFDFPGTSASREMFLADIRGCEITPRPIGETVPLGMVM
SAPLGDGVDRIIVCERGAPARRRTGPPPYQEVAAAWQRLTGQDISHGEPV
WVSAFGDPARQVSAYRRGRVLLAGDSAHVHLPAGGQGMNVSVQDSVNLGW
KLAAVVSGRAPAGLLDTYHEERHPVGRRLLMNTQAQGMLFLSGDEMQPLR
DVLSELIRYDEVSRHLAGMVSGLDIRYEVDGGDHPLLGMRMPHQELVRAH
GKTSTTELLHPARGVLLDIADDAEVREAATGWSDRVDIVTASLHDAPPQG
PLSDARAVLVRPDGYVAWISPGSRAGLTEALDRWFGPAR

3D structure

• PDB: 2qa2 Crystal structures of two aromatic hydroxylases involved in the early tailoring steps of angucycline biosynthesis
• Chain: A
• Resolution: 2.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): L44 E67 L204 I212 P282
• Catalytic site (residue number reindexed from 1): L44 E67 L204 I212 P282
• Enzyme Commision number: 1.14.13.-

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	FAD	A	G9 G11 P12 A13 E32 Q33 R42 G43 Q96 V120 D152 G153 T157 G274 D275 P282 G285 Q286 G287 M288 N289	G9 G11 P12 A13 E32 Q33 R42 G43 Q96 V120 D152 G153 T157 G274 D275 P282 G285 Q286 G287 M288 N289

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0016491 oxidoreductase activity
• GO:0016709 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
• GO:0071949 FAD binding

External links

• PDB: RCSB:2qa2, PDBe:2qa2, PDBj:2qa2
• PDBsum: 2qa2
• PubMed: 17669423
• UniProt: D0VWY3