Structure of PDB 6a17 Chain A

Receptor sequence
>6a17A (length=444) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
RFNLPPGKSGWPFLGETIGYLKPYTATTLGDFMQQHVSKYGKIYRSNLFG
EPTIVSADAGLNRFILQNEGRLFECSYPRSIGGILGKWSMLVLVGDMHRD
MRSISLNFLSHARLRTILLKDVERHTLFVLDSWQQNSIFSAQDEAKKFTF
NLMAKHIMSMDPGEEETEQLKKEYVTFMKGVVSAPLNLPGTAYHKALQSR
ATILKFIERKMEERKLDIKERKQRTDDDLLGWVLKHSNLSTEQILDLILS
LLFAGHETSSVAIALAIFFLQACPKAVEELREEHLEIARAKKELGESELN
WDDYKKMDFTQCVINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLP
VISAVHLDNSRYDQPNLFNPWRWQQQNTWGNNYMPFGGGPRLCAGSELAK
LEMAVFIHHLVLKFNWELAEDDKPFAFPFVDFPNGLLIRVSRIL
3D structure
PDB6a17 Structural insights into a key step of brassinosteroid biosynthesis and its inhibition.
ChainA
Resolution2.301 Å
3D
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
Enzyme Commision number 1.14.14.178: steroid 22S-hydroxylase.
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 9RL A Y112 L120 L126 V216 S307 A311 T315 Y77 L85 L91 V181 S250 A254 T258 MOAD: Ki=1.05uM
BS02 HEM A Y112 M125 H133 R137 G312 T315 V381 L384 R386 P454 F455 R460 C462 A468 Y77 M90 H98 R102 G255 T258 V324 L327 R329 P385 F386 R391 C393 A399
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding

View graph for
Molecular Function
External links
PDB RCSB:6a17, PDBe:6a17, PDBj:6a17
PDBsum6a17
PubMed31182839
UniProtO64989|C90B1_ARATH Steroid (22S)-hydroxylase (Gene Name=CYP90B1)

[Back to BioLiP]