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1NV8

N5-glutamine methyltransferase, HemK

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0006415biological_processtranslational termination
A0006479biological_processprotein methylation
A0008168molecular_functionmethyltransferase activity
A0008170molecular_functionN-methyltransferase activity
A0008276molecular_functionprotein methyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0016740molecular_functiontransferase activity
A0032259biological_processmethylation
A0036009molecular_functionprotein-glutamine N-methyltransferase activity
A0102559molecular_functionpeptide chain release factor N(5)-glutamine methyltransferase activity
B0003676molecular_functionnucleic acid binding
B0006415biological_processtranslational termination
B0006479biological_processprotein methylation
B0008168molecular_functionmethyltransferase activity
B0008170molecular_functionN-methyltransferase activity
B0008276molecular_functionprotein methyltransferase activity
B0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
B0016740molecular_functiontransferase activity
B0032259biological_processmethylation
B0036009molecular_functionprotein-glutamine N-methyltransferase activity
B0102559molecular_functionpeptide chain release factor N(5)-glutamine methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE SAM A 300
ChainResidue
APHE100
AASN197
APRO199
AGLU217
AALA218
AMEQ400
AHOH401
AHOH402
AHOH404
AHOH408
AHOH464
APRO102
AHOH467
AGLY129
ATHR130
AGLY131
AASP151
AVAL152
AGLU179
APHE180

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SAM B 301
ChainResidue
BPHE100
BPRO102
BGLY129
BTHR130
BGLY131
BASP151
BVAL152
BGLY178
BGLU179
BPHE180
BASN197
BPRO199
BGLU217
BALA218
BMEQ401
BHOH406
BHOH407
BHOH409
BHOH410
BHOH436
BHOH488

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MEQ A 400
ChainResidue
AARG103
AASN197
APRO198
APRO199
ATYR200
AVAL201
AALA218
ALEU219
ASAM300

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MEQ B 401
ChainResidue
BASN197
BPRO198
BPRO199
BTYR200
BLEU219
BSAM301

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 Residues14
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18247349","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of N5-glutamine methyltransferase, HemK(EC 2.1.1.-) (TM0488) from Thermotoga maritima at 2.80 A resolution.","authoringGroup":["Joint Center for Structural Genomics (JCSG)"]}}]}
ChainResidueDetails

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

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qam
ChainResidueDetails
BASP151
BASN197
BGLY129

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

site_idMCSA2
Number of Residues3
DetailsM-CSA 703
ChainResidueDetails
BPHE100electrostatic stabiliser
BASN197electrostatic stabiliser
BPRO198electrostatic stabiliser

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PDB entries from 2026-01-14

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