Structure of PDB 4kic Chain B

Receptor sequence

>4kicB (length=332) Species: 1912 (Streptomyces hygroscopicus)

SEAQARRAVADIFNSTLASSAIGAAWELGALDELRENGKLDVSDFAVRHD
LHEPAVVGMFTALASVGIVRREGATVVVGPYFDEANHHRSLFHWLNQGSG
ELFRRMPQVLPNENRTGKFYQRDAGAISYACREISERYFDPAFWAAVDGL
GYTPTTVADLGSGSGERLIQIARRFPGVRGLGVDIADGAIAMAEKEVAAK
GFGDQISFVRGDARTIDQVSARGEFAEVDLLTCFMMGHDFWPRENCVQTL
RKLRAAFPNVRRFLLGDATRTVGIPDRELPVFTLGFEFGHDMMGVYLPTL
DEWDGVFEEGGWRCVKKHAIDSLSVSVVFELE

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: B
• 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	CA	B	R127 D128	R122 D123
BS02	SAM	B	C136 G166 D189 I190 D217 A218 R219 M240 M241 D244	C131 G161 D184 I185 D212 A213 R214 M235 M236 D239
BS03	PPY	B	W99 R127 M240 H243 F287 F291 H295	W94 R122 M235 H238 F282 F286 H290
BS04	FE	B	H243 H295	H238 H290
BS05	HF2	B	D309 C319 K322	D304 C314 K317
BS06	CA	B	K44 L45	K39 L40
BS07	CA	B	Q223 V224	Q218 V219
BS08	CA	B	T220 D222 K257	T215 D217 K252

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)