Structure of PDB 1t6y Chain B

Receptor sequence
>1t6yB (length=270) Species: 2336 (Thermotoga maritima) [Search protein sequence]
VVSIGVFDGVHIGHQKVLRTMKEIAFFRKDDSLIYTISYPPEYFLPDFPG
LLMTVESRVEMLSRYARTVVLDFFRIKDLTPEGFVERYLSGVSAVVVGRD
FRFGKNASGNASFLRKKGVEVYEIEDVVVQGKRVSSSLIRNLVQEGRVEE
IPAYLGRYFEIEGIVHFPTANIDRGNEKLVDLKRGVYLVRVHLPDGKKKF
GVMNVGFNVKYEVYILDFEGDLYGQRLKLEVLKFMRDEKKFDSIEELKAA
IDQDVKSARNMIDDIINSKF
3D structure
PDB1t6y Crystal structure of ADP bound FAD synthetase
ChainB
Resolution2.8 Å
3D
structure
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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 B P479 T480 A481 Y533 I534 G539 L541 P168 T169 A170 Y214 I215 G220 L222
BS02 AMP B V307 H315 V318 V398 G399 D427 V428 V435 V6 H14 V17 V97 G98 D126 V127 V134
BS03 FMN B V497 N515 F518 K529 E531 R555 E557 K558 L566 V186 N204 F207 K210 E212 R236 E238 K239 L247
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

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

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