Structure of PDB 4kri Chain A

Receptor sequence
>4kriA (length=429) Species: 6289 (Haemonchus contortus) [Search protein sequence]
ASMPAVERQLIECLHHVIKGAEPQQVGILCPQDDQRKALTEQFGSKTATS
FCKEVDSLKNLSNLDALIVNQALDEEINDSEKLDKFITAALRSLRTDGVL
ILRQDLSKVKEMKKMAMLTDYFDVFRLEEGNGNVGFQFYAVNEVLDSVYV
HQNWLDFIWTLMKKPFPKVVSFRDFLDRTQYTDTGIFAYEWIFGNNFISP
GGWNQNLAILKRFGPMKTGQRMLDIGVGIGGGARQAASEFGLQVHGVDLS
TNMLAVALERVHKEKDARVTYAVCDACEYEFEPNSFDYVFSRDCIQHIKD
TDKLFSRIYRALKPGGKVLITMYGVGHGTLSESFKEYVSQRQYYLKNLEQ
IEEIAKKTGFIDIEVENMTPRFKEILLEERERIEQDKETFLAKFSQNAYD
GLVSGWKSKLQYIADDNHNWNFFAAVKPQ
3D structure
PDB4kri Evolution of structure and mechanistic divergence in di-domain methyltransferases from nematode phosphocholine biosynthesis.
ChainA
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 A Y183 I200 S201 G228 V229 G230 D250 L251 M255 D277 A278 R294 C296 H299 I300 Y181 I198 S199 G226 V227 G228 D248 L249 M253 D275 A276 R292 C294 H297 I298
BS02 1SH A Y191 Y325 Y339 R343 Y345 K411 Y189 Y323 Y337 R341 Y343 K409
Gene Ontology
Molecular Function
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0016740 transferase activity
Biological Process
GO:0009058 biosynthetic process

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Molecular Function

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Biological Process
External links
PDB RCSB:4kri, PDBe:4kri, PDBj:4kri
PDBsum4kri
PubMed24012478
UniProtU5HK48

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