Structure of PDB 4kig Chain B

Receptor sequence
>4kigB (length=332) Species: 1912 (Streptomyces hygroscopicus) [Search protein sequence]
SEAQARRAVADIFNSTLASSAIGAAWELGALDELRENGKLDVSDFAVRHD
LHEPAVVGMFTALASVGIVRREGATVVVGPYFDEANHHRSLFHWLNQGSG
ELFRRMPQVLPNENRTGKFYQRDAGAISYACREISERYFDPAFWAAVDGL
GYTPTTVADLGSGSGERLIQIARRFPGVRGLGVDIADGAIAMAEKEVAAK
GFGDQISFVRGDARTIDQVSARGEFAEVDLLTCFMMGHDFWPRENCVQTL
RKLRAAFPNVRRFLLGDATRTVGIPDRELPVFTLGFEFGHDMMGVYLPTL
DEWDGVFEEGGWRCVKKHAIDSLSVSVVFELE
3D structure
PDB4kig Structure and mechanism of a nonhaem-iron SAM-dependent C-methyltransferase and its engineering to a hydratase and an O-methyltransferase
ChainB
Resolution2.4 Å
3D
structure
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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 E106 Q126 R127 D128 E101 Q121 R122 D123
BS02 ENO B W99 R127 F144 M240 H243 A273 F287 F291 H295 W94 R122 F139 M235 H238 A268 F282 F286 H290
BS03 FE B H243 H295 H238 H290
BS04 34H B D309 F312 C319 V320 K321 K322 D304 F307 C314 V315 K316 K317
BS05 CA B F180 P181 G182 F175 P176 G177
BS06 CA B R248 E249 R243 E244
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
Biological Process
GO:0009058 biosynthetic process
GO:0017000 antibiotic biosynthetic process
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:4kig, PDBe:4kig, PDBj:4kig
PDBsum4kig
PubMed24914966
UniProtQ643C8|MPPJ_STRHY Phenylpyruvate C(3)-methyltransferase (Gene Name=mppJ)

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