Structure of PDB 1kr5 Chain A

Receptor sequence
>1kr5A (length=218) Species: 9606 (Homo sapiens) [Search protein sequence]
ASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKCNPYMDSPQSIGFQA
TISAPHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGCTGKVI
GIDHIKELVDDSVNNVRKDDPTLLSSGRVQLVVGDGRMGYAEEAPYDAIH
VGAAAPVVPQALIDQLKPGGRLILPVGPAGGNQMLEQYDKLQDGSIKMKP
LMGVIYVPLTDKEKQWSR
3D structure
PDB1kr5 Crystal structure of human L-isoaspartyl methyltransferase.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S59
Catalytic site (residue number reindexed from 1) S53
Enzyme Commision number 2.1.1.77: protein-L-isoaspartate(D-aspartate) O-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 A56 T57 I58 H64 G85 S86 G87 S88 D109 H110 D141 G142 L215 T216 Q221 A50 T51 I52 H58 G79 S80 G81 S82 D103 H104 D135 G136 L209 T210 Q215
Gene Ontology
Molecular Function
GO:0004719 protein-L-isoaspartate (D-aspartate) O-methyltransferase activity
GO:0005515 protein binding
GO:0008168 methyltransferase activity
GO:0045296 cadherin binding
Biological Process
GO:0006479 protein methylation
GO:0030091 protein repair
GO:0032259 methylation
GO:0036211 protein modification process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome
GO:1903561 extracellular vesicle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1kr5, PDBe:1kr5, PDBj:1kr5
PDBsum1kr5
PubMed11792715
UniProtP22061|PIMT_HUMAN Protein-L-isoaspartate(D-aspartate) O-methyltransferase (Gene Name=PCMT1)

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