Structure of PDB 4m3p Chain D

Receptor sequence
>4m3pD (length=371) Species: 9606 (Homo sapiens) [Search protein sequence]
KKGILERLNAGEIVIGDGGFVFALEKRGYVKAGPWTPEAAVEHPEAVRQL
HREFLRAGSNVMQTFTFYSGQEVNEAACDIARQVADEGDALVAGGVSQTP
SYLSCKSETEVKKVFLQQLEVFMKKNVDFLIAEYFEHVEEAVWAVETLIA
SGKPVAATMCIGPEGDLHGVPPGECAVRLVKAGASIIGVNCHFDPTISLK
TVKLMKEGLEAAQLKAHLMSQPLAYHTPDCNKQGFIDLPEFPFGLEPRVA
TRWDIQKYAREAYNLGVRYIGGCCGFEPYHIRAIAEELAPERGFLPPASE
KHGSWGSGLDMHTKPWVRARARKEYWENLRIASGRPYNPSMSKPDGWAEL
MQQKEATTEQQLKELFEKQKF
3D structure
PDB4m3p Specific potassium ion interactions facilitate homocysteine binding to betaine-homocysteine S-methyltransferase.
ChainD
Resolution1.895 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.1.1.5: betaine--homocysteine S-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 ZN D C217 C299 C191 C273
BS02 K D D26 G27 Q72 Q247 G298 C299 D17 G18 Q63 Q221 G272 C273
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008172 S-methyltransferase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
GO:0047150 betaine-homocysteine S-methyltransferase activity
Biological Process
GO:0006479 protein methylation
GO:0006577 amino-acid betaine metabolic process
GO:0006579 amino-acid betaine catabolic process
GO:0009086 methionine biosynthetic process
GO:0032259 methylation
GO:0046500 S-adenosylmethionine metabolic process
GO:0050666 regulation of homocysteine metabolic process
GO:0071266 'de novo' L-methionine biosynthetic process
GO:0071267 L-methionine salvage
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4m3p, PDBe:4m3p, PDBj:4m3p
PDBsum4m3p
PubMed24895213
UniProtQ93088|BHMT1_HUMAN Betaine--homocysteine S-methyltransferase 1 (Gene Name=BHMT)

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