Structure of PDB 4kib Chain A

Receptor sequence

>4kibA (length=333) Species: 1912 (Streptomyces hygroscopicus)

VSEAQARRAVADIFNSTLASSAIGAAWELGALDELRENGKLDVSDFAVRH
DLHEPAVVGMFTALASVGIVRREGATVVVGPYFDEANHHRSLFHWLNQGS
GELFRRMPQVLPNENRTGKFYQRDAGAISYACREISERYFDPAFWAAVDG
LGYTPTTVADLGSGSGERLIQIARRFPGVRGLGVDIADGAIAMAEKEVAA
KGFGDQISFVRGDARTIDQVSARGEFAEVDLLTCFMMGHDFWPRENCVQT
LRKLRAAFPNVRRFLLGDATRTVGIPDRELPVFTLGFEFGHDMMGVYLPT
LDEWDGVFEEGGWRCVKKHAIDSLSVSVVFELE

3D structure

• PDB: 4kib Structure and mechanism of a nonhaem-iron SAM-dependent C-methyltransferase and its engineering to a hydratase and an O-methyltransferase
• Chain: A
• Resolution: 2.0 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	SAH	A	C136 G166 G168 D189 I190 G216 D217 A218 R219 F239 M240 M241	C132 G162 G164 D185 I186 G212 D213 A214 R215 F235 M236 M237
BS02	56D	A	W99 R127 M240 H243 F287 H295	W95 R123 M236 H239 F283 H291
BS03	FE	A	H243 H295	H239 H291
BS04	HF2	A	D309 F312 C319 K321 K322	D305 F308 C315 K317 K318
BS05	CA	A	G216 D217	G212 D213
BS06	CA	A	F180 P181 G182	F176 P177 G178
BS07	CA	A	E106 R127 D128	E102 R123 D124

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