Structure of PDB 4kri Chain C

Receptor sequence
>4kriC (length=427) Species: 6289 (Haemonchus contortus) [Search protein sequence]
ASMPAVERQLIECLHHVIKGAEPQQVGILCPQDDQRKALTEQFGSKTATS
FCKEVDSLKNLSNLDALIVNQALDEEINDSEKLDKFITAALRSLRTDGVL
ILRQDLSKVKEMKKMAMLTDYFDVFRLEEGNGNVGFQFYAVNEVLDSVYV
HQNWLDFIWTLMKKPFPVSFRDFLDRTQYTDTGIFAYEWIFGNNFISPGG
WNQNLAILKRFGPMKTGQRMLDIGVGIGGGARQAASEFGLQVHGVDLSTN
MLAVALERVHKEKDARVTYAVCDACEYEFEPNSFDYVFSRDCIQHIKDTD
KLFSRIYRALKPGGKVLITMYGVGHGTLSESFKEYVSQRQYYLKNLEQIE
EIAKKTGFIDIEVENMTPRFKEILLEERERIEQDKETFLAKFSQNAYDGL
VSGWKSKLQYIADDNHNWNFFAAVKPQ
3D structure
PDB4kri Evolution of structure and mechanistic divergence in di-domain methyltransferases from nematode phosphocholine biosynthesis.
ChainC
Resolution1.72 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.1.1.103: phosphoethanolamine N-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 C F174 I200 S201 G228 V229 G230 D250 L251 M255 D277 R294 C296 H299 F170 I196 S197 G224 V225 G226 D246 L247 M251 D273 R290 C292 H295
BS02 1SH C Y191 Y325 Y339 R343 Y345 K411 Y187 Y321 Y335 R339 Y341 K407
Gene Ontology
Molecular Function
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0016740 transferase activity
Biological Process
GO:0009058 biosynthetic process

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:4kri, PDBe:4kri, PDBj:4kri
PDBsum4kri
PubMed24012478
UniProtU5HK48

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