Structure of PDB 4s2a Chain A

Receptor sequence
>4s2aA (length=594) Species: 190650 (Caulobacter vibrioides CB15) [Search protein sequence]
STGPIPGSRKVYQAGELFPELRVPFREVAVHPSANEPPVTIYDPSGPYSD
PAIQIDIEKGLPRTREALVVARGDVEEVADPRQVKPEDNGFAQGKHLAPE
FPDTGRKIYRAKPGKLVTQLEYARAGIITAEMEYVAIRENLRREQDRPCV
RDGEDFGASIPDFVTPEFVRQEIARGRAIIPANINHGELEPMAIGRNFLV
KINANIGNSTVADEVDKLVWATRWGADTVMDLSTGRNIHNIRDWIIRNSS
VPIGTVPIYQALEKVNGVAEDLNWEVFRDTLIEQCEQGVDYFTIHAGVRL
PFIPMTAKRVTGIVSRGGSIMAKWCLAHHKENFLYERFDEICEIMRAYDV
SFSLGDGLRPGSTADANDEAQFSELRTLGELTKVAWKHGVQVMIEGPGHV
AMHKIKANMDEQLKHCHEAPFYTLGPLTTDIAPGYDHITSAIGAAMIGWF
GTAMLCYVTPKEHLGLPDRDDVKTGVITYKLAAHAADLAKGHPGAAMWDD
AISRARFEFRWEDQFNLGLDPETARKFHDETLPKEAHKTAHFCSMCGPKF
CSMKISQEVRDFAAGKAPNSAELGMAEMSEKFREQGSEIYLKTE
3D structure
PDB4s2a Non-canonical active site architecture of the radical SAM thiamin pyrimidine synthase.
ChainA
Resolution2.93 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.99.17: phosphomethylpyrimidine 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 SF4 A F560 C561 C564 F568 C569 F542 C543 C546 F550 C551
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0016830 carbon-carbon lyase activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
GO:0070284 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity
Biological Process
GO:0009228 thiamine biosynthetic process
GO:0009229 thiamine diphosphate biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:4s2a, PDBe:4s2a, PDBj:4s2a
PDBsum4s2a
PubMed25813242
UniProtQ9A6Q5|THIC_CAUVC Phosphomethylpyrimidine synthase (Gene Name=thiC)

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