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PDBsum entry 5e1m

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protein ligands Protein-protein interface(s) links
Transferase PDB id
5e1m

 

 

 

 

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Contents
Protein chains
227 a.a.
Ligands
PRO-PRO-LYS-ARG-
ILE-ALA
×2
SAH ×2
GOL ×3
UNX ×43
Waters ×417
PDB id:
5e1m
Name: Transferase
Title: Crystal structure of ntmt1 in complex with ppkria peptide
Structure: N-terminal xaa-pro-lys n-methyltransferase 1. Chain: a, b. Synonym: alpha n-terminal protein methyltransferase 1a, methyltransferase-like protein 11a,n-terminal rcc1 methyltransferase, x-pro-lys n-terminal protein methyltransferase 1a,ntm1a. Engineered: yes. Rcc1. Chain: d, e. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ntmt1, c9orf32, mettl11a, nrmt, nrmt1, ad-003. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Other_details: synthetic peptide
Resolution:
1.75Å     R-factor:   0.162     R-free:   0.188
Authors: C.Dong,W.Tempel,C.Bountra,C.H.Arrowsmith,A.M.Edwards,J.Min,Structural Genomics Consortium (Sgc)
Key ref: C.Dong et al. (2015). Structural basis for substrate recognition by the human N-terminal methyltransferase 1. Genes Dev, 29, 2343-2348. PubMed id: 26543161 DOI: 10.1101/gad.270611.115
Date:
29-Sep-15     Release date:   28-Oct-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9BV86  (NTM1A_HUMAN) -  N-terminal Xaa-Pro-Lys N-methyltransferase 1 from Homo sapiens
Seq:
Struc:
223 a.a.
227 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.1.1.244  - protein N-terminal methyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L- methionine = N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl- [protein] + 3 S-adenosyl-L-homocysteine + 3 H+
2. N-terminal L-seryl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L- methionine = N-terminal N,N,N-trimethyl-L-seryl-L-prolyl-L-lysyl- [protein] + 3 S-adenosyl-L-homocysteine + 3 H+
3. N-terminal L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl-L- methionine = N-terminal N,N-dimethyl-L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl-L-homocysteine + 2 H+
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein]
+ 3 × S-adenosyl-L- methionine
= N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl- [protein]
+ 3 × S-adenosyl-L-homocysteine
+ 3 × H(+)
Bound ligand (Het Group name = SAH)
corresponds exactly
N-terminal L-seryl-L-prolyl-L-lysyl-[protein]
+ 3 × S-adenosyl-L- methionine
= N-terminal N,N,N-trimethyl-L-seryl-L-prolyl-L-lysyl- [protein]
+ 3 × S-adenosyl-L-homocysteine
+ 3 × H(+)
Bound ligand (Het Group name = SAH)
corresponds exactly
N-terminal L-prolyl-L-prolyl-L-lysyl-[protein]
+ 2 × S-adenosyl-L- methionine
= N-terminal N,N-dimethyl-L-prolyl-L-prolyl-L-lysyl-[protein]
+ 2 × S-adenosyl-L-homocysteine
+ 2 × H(+)
Bound ligand (Het Group name = SAH)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1101/gad.270611.115 Genes Dev 29:2343-2348 (2015)
PubMed id: 26543161  
 
 
Structural basis for substrate recognition by the human N-terminal methyltransferase 1.
C.Dong, Y.Mao, W.Tempel, S.Qin, L.Li, P.Loppnau, R.Huang, J.Min.
 
  ABSTRACT  
 
No abstract given.

 

 

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