Structure of PDB 1jqd Chain A

Receptor sequence
>1jqdA (length=286) Species: 9606 (Homo sapiens) [Search protein sequence]
MRSLFHGKYVESFRRFLNHSTEHQCMQEFMDKKLPGIIGRIGDTKSEIKI
LSIGGGAGEIDLQILSKVQAQYPGVCINNEVVEPSAEQIAKYKELVAKTS
NLENVKFAWHKETSSEYQSRMLEKKELQKWDFIHMIQMLYYVKDIPATLK
FFHSLLGTNAKMLIIVVSGSSGWDKLWKKYGSRFPQDDLCQYITSDDLTQ
MLDNLGLKYECYDLLSTMDISDCFIDGNENGDLLWDFLTETCNFNATAPP
DLRAELGKDLQEPEFSAKKEGKVLFNNTLSFIVIEA
3D structure
PDB1jqd Two polymorphic forms of human histamine methyltransferase: structural, thermal, and kinetic comparisons.
ChainA
Resolution2.28 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.1.1.8: histamine 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 G60 E89 P90 Q94 T119 S120 I142 Q143 M144 Y147 G54 E83 P84 Q88 T113 S114 I136 Q137 M138 Y141 MOAD: Ki=6.9uM
PDBbind-CN: -logKd/Ki=5.16,Ki=6.9uM
BindingDB: Ki=18100nM
BS02 HSM A F22 E28 Q143 N283 F16 E22 Q137 N277
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008170 N-methyltransferase activity
GO:0046539 histamine N-methyltransferase activity
Biological Process
GO:0001692 histamine metabolic process
GO:0001695 histamine catabolic process
GO:0006548 L-histidine catabolic process
GO:0007585 respiratory gaseous exchange by respiratory system
GO:0032259 methylation
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005813 centrosome
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:1jqd, PDBe:1jqd, PDBj:1jqd
PDBsum1jqd
PubMed11566133
UniProtP50135|HNMT_HUMAN Histamine N-methyltransferase (Gene Name=HNMT)

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