Structure of PDB 4kic Chain A

Receptor sequence

>4kicA (length=334) Species: 1912 (Streptomyces hygroscopicus)

EVSEAQARRAVADIFNSTLASSAIGAAWELGALDELRENGKLDVSDFAVR
HDLHEPAVVGMFTALASVGIVRREGATVVVGPYFDEANHHRSLFHWLNQG
SGELFRRMPQVLPNENRTGKFYQRDAGAISYACREISERYFDPAFWAAVD
GLGYTPTTVADLGSGSGERLIQIARRFPGVRGLGVDIADGAIAMAEKEVA
AKGFGDQISFVRGDARTIDQVSARGEFAEVDLLTCFMMGHDFWPRENCVQ
TLRKLRAAFPNVRRFLLGDATRTVGIPDRELPVFTLGFEFGHDMMGVYLP
TLDEWDGVFEEGGWRCVKKHAIDSLSVSVVFELE

3D structure

• PDB: 4kic Structure and mechanism of a nonhaem-iron SAM-dependent C-methyltransferase and its engineering to a hydratase and an O-methyltransferase
• Chain: A
• Resolution: 2.43 Å

Enzymatic activity

• Enzyme Commision number: 2.1.1.281: phenylpyruvate C(3)-methyltransferase.

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	SAM	A	C136 G166 G168 D189 I190 G216 D217 A218 F239 M240 M241 D244	C133 G163 G165 D186 I187 G213 D214 A215 F236 M237 M238 D241
BS02	PPY	A	W99 R127 M240 H243 A273 F287 F291 H295	W96 R124 M237 H240 A270 F284 F288 H292
BS03	FE	A	H243 D244 H295	H240 D241 H292
BS04	HF2	A	D309 F312 C319 F334	D306 F309 C316 F331
BS05	CA	A	E106 R127 D128	E103 R124 D125
BS06	CA	A	K123 Y125	K120 Y122

Gene Ontology

Molecular Function

• GO:0008168 methyltransferase activity

Biological Process

• GO:0009058 biosynthetic process
• GO:0017000 antibiotic biosynthetic process
• GO:0032259 methylation

External links

• PDB: RCSB:4kic, PDBe:4kic, PDBj:4kic
• PDBsum: 4kic
• PubMed: 24914966
• UniProt: Q643C8|MPPJ_STRHY Phenylpyruvate C(3)-methyltransferase (Gene Name=mppJ)