BioLiP

Structure of PDB 1jg3 Chain B Binding Site BS01

Receptor Information

>1jg3 Chain B (length=215) Species: 2261 (Pyrococcus furiosus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

EKELYEKWMRTVEMLKAEGIIRSKEVERAFLKYPRYLSVEDKYKKYAHID
EPLPIPAGQTVSAPHMVAIMLEIANLKPGMNILEVGTGSGWNAALISEIV
KTDVYTIERIPELVEFAKRNLERAGVKNVHVILGDGSKGFPPKAPYDVII
VTAGAPKIPEPLIEQLKIGGKLIIPVGSYHLWQELLEVRKTKDGIKIKNH
GGVAFVPLIGEYGWK

Ligand information

>1jg3 Chain D (length=6) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

VYPDHA

Receptor-Ligand Complex Structure

Global view

Local view

Structure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

PDB	1jg3 Crystal structure of a protein repair methyltransferase from Pyrococcus furiosus with its L-isoaspartyl peptide substrate.
Resolution	2.1 Å
Binding residue (original residue number in PDB)	P65 P67 T73 S75 A76 H78 M79 V216 A217 F218 V219
Binding residue (residue number reindexed from 1)	P52 P54 T60 S62 A63 H65 M66 V203 A204 F205 V206

Enzymatic activity

Catalytic site (original residue number in PDB)	S75
Catalytic site (residue number reindexed from 1)	S62
Enzyme Commision number	2.1.1.77: protein-L-isoaspartate(D-aspartate) O-methyltransferase.

Gene Ontology

	Molecular Function
GO:0004719	protein-L-isoaspartate (D-aspartate) O-methyltransferase activity
GO:0008168	methyltransferase activity
GO:0016740	transferase activity

	Biological Process
GO:0030091	protein repair
GO:0032259	methylation
GO:0036211	protein modification process

	Cellular Component
GO:0005737	cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

PDB	RCSB:1jg3, PDBe:1jg3, PDBj:1jg3
PDBsum	1jg3
PubMed	11700066
UniProt	Q8TZR3\|PIMT_PYRFU Protein-L-isoaspartate O-methyltransferase (Gene Name=pcm)