Structure of PDB 1t6y Chain A

Receptor sequence
>1t6yA (length=268) Species: 2336 (Thermotoga maritima) [Search protein sequence]
VVSIGVFDGVHIGHQKVLRTMKEIAFFRKDDSLIYTISYPPEYFLPDFPG
LLMTVESRVEMLSRYARTVVLDFFRIKDLTPEGFVERYLSGVSAVVVGRD
FRFGKNASGNASFLRKKGVEVYEIEDVVVQGKRVSSSLIRNLVQEGRVEE
IPAYLGRYFEIEGIVHKFPTANIDRGNEKLVDLKRGVYLVRVHLPDGKKK
FGVMNVGFRRNVKYEVYILDFEGDLYGQRLKLEVLKFMRDEKKEELKAAI
DQDVKSARNMIDDIINSK
3D structure
PDB1t6y Crystal structure of ADP bound FAD synthetase
ChainA
Resolution2.8 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 2.7.1.26: riboflavin kinase.
2.7.7.2: FAD 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 ADP A H167 P179 T180 I234 D240 L241 H166 P169 T170 I218 D224 L225
BS02 AMP A V7 H15 V18 G99 D101 D127 V128 V135 V6 H14 V17 G98 D100 D126 V127 V134
BS03 FMN A F178 V197 V213 N215 K229 E231 R255 E257 K258 L266 I270 F168 V187 V203 N205 K213 E215 R239 E241 K242 L246 I250
Gene Ontology
Molecular Function
GO:0003919 FMN adenylyltransferase activity
GO:0005524 ATP binding
GO:0008531 riboflavin kinase activity
GO:0016301 kinase activity
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006747 FAD biosynthetic process
GO:0006771 riboflavin metabolic process
GO:0009231 riboflavin biosynthetic process
GO:0009398 FMN biosynthetic process
GO:0016310 phosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1t6y, PDBe:1t6y, PDBj:1t6y
PDBsum1t6y
PubMed
UniProtQ9WZW1

[Back to BioLiP]