1or8 Summary

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Structure of the Predominant protein arginine methyltransferase PRMT1

The structure was published by Zhang, X. and Cheng, X., in 2003 in a paper entitled "Structure of the Predominant Protein Arginine Methyltransferase PRMT1 and Analysis of Its Binding to Substrate Peptides" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.35 Å and deposited in 2003.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely Protein arginine N-methyltransferase 1 and Substrate peptide.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Protein arginine N-methyltransferase 1 Q63009 (14-353) (ANM1_RAT)search Rattus norvegicussearch 96% 340 92%
B Substrate peptide Not available
Synthetic Not available 19 78%
C Substrate peptide Not available
Synthetic Not available 19 78%
D Substrate peptide Not available
Synthetic Not available 19 78%
E Substrate peptide Not available
Synthetic Not available 19 78%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q63009 (14 - 353) Protein arginine N-methyltransferase 1 Rattus norvegicus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (Q63009) Arginine methyltransferasesearch Vaccinia Virus protein VP39search, Hnrnp arginine n-methyltransferase1search PF13847: Methyltransferase domainsearch
B, C, D, E

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (Q63009) protein bindingsearch protein methyltransferase activitysearch histone methyltransferase activitysearch identical protein bindingsearch protein-arginine omega-N asymmetric methyltransferase activitysearch methyltransferase activitysearch histone-arginine N-methyltransferase activitysearch protein-arginine omega-N monomethyltransferase activitysearch histone methyltransferase activity (H4-R3 specific)search transferase activitysearch S-adenosylmethionine-dependent methyltransferase activitysearch [cytochrome c]-arginine N-methyltransferase activitysearch snoRNP bindingsearch N-methyltransferase activitysearch poly(A) RNA bindingsearch protein-arginine N-methyltransferase activitysearch nucleoplasmsearch cytosolsearch nucleussearch cytoplasmsearch protein complexsearch methylationsearch histone H4-R3 methylationsearch protein methylationsearch negative regulation of megakaryocyte differentiationsearch peptidyl-arginine methylation, to asymmetrical-dimethyl argininesearch liver regenerationsearch peptidyl-arginine methylationsearch in utero embryonic developmentsearch regulation of transcription, DNA-templatedsearch histone methylationsearch neuron projection developmentsearch peptidyl-arginine omega-N-methylationsearch

Chain InterPro annotation
A Methyltransferase domainsearch Protein arginine N-methyltransferasesearch S-adenosyl-L-methionine-dependent methyltransferasesearch
B, C, D, E