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1NV9

HemK, apo structure

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0006479biological_processprotein methylation
A0008168molecular_functionmethyltransferase activity
A0008170molecular_functionN-methyltransferase activity
A0008276molecular_functionprotein methyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0018364biological_processpeptidyl-glutamine methylation
A0032259biological_processmethylation
A0036009molecular_functionprotein-glutamine N-methyltransferase activity
A0043414biological_processmacromolecule methylation
A0102559molecular_functionprotein-(glutamine-N5) methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SAH A 300
ChainResidue
APHE100
APRO199
AGLU217
AALA218
AHOH304
AHOH319
APRO102
AGLY129
ATHR130
AGLY131
AASP151
AGLU179
APHE180
AASN197

Functional Information from PROSITE/UniProt
site_idPS00092
Number of Residues7
DetailsN6_MTASE N-6 Adenine-specific DNA methylases signature. ILSNPPY
ChainResidueDetails
AILE194-TYR200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AGLY129

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18247349, ECO:0000269|Ref.5
ChainResidueDetails
AASP151
APHE180
AASN197

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qam
ChainResidueDetails
AASP151
AASN197
AGLY129

site_idMCSA1
Number of Residues3
DetailsM-CSA 703
ChainResidueDetails
APHE100electrostatic stabiliser
AASN197electrostatic stabiliser
APRO198electrostatic stabiliser

224572

PDB entries from 2024-09-04

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