Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5X62

Crystal structure of a carnosine N-methyltransferase bound by AdoHcy

Functional Information from GO Data
ChainGOidnamespacecontents
A0005575cellular_componentcellular_component
A0008168molecular_functionmethyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0030735molecular_functioncarnosine N-methyltransferase activity
A0032259biological_processmethylation
A0035498biological_processcarnosine metabolic process
B0005575cellular_componentcellular_component
B0008168molecular_functionmethyltransferase activity
B0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
B0030735molecular_functioncarnosine N-methyltransferase activity
B0032259biological_processmethylation
B0035498biological_processcarnosine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue SAH A 501
ChainResidue
AGLN108
ASER234
APHE235
AASN274
APHE275
ATHR279
ATYR286
ATYR371
AHOH601
AHOH664
AARG111
AGLY146
AASN166
AGLU167
APHE168
ASER169
AMET172
AGLY233

site_idAC2
Number of Residues21
Detailsbinding site for residue SAH B 501
ChainResidue
BGLN108
BARG111
BGLY146
BGLY148
BASN166
BGLU167
BPHE168
BSER169
BMET172
BGLY233
BSER234
BPHE235
BASN274
BPHE275
BPHE276
BTHR279
BTYR286
BTYR371
BHOH605
BHOH651
BHOH670

site_idAC3
Number of Residues6
Detailsbinding site for residue NA B 502
ChainResidue
BASN266
BGLY291
BHIS292
BLEU294
BHOH700
BHOH704

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8N4J0
ChainResidueDetails
AGLN108
AARG111
AGLY146
AGLU167
APHE235
AASP278
ATYR286
AHIS309
ATYR385
BGLN108
BARG111
BGLY146
BGLU167
BPHE235
BASP278
BTYR286
BHIS309
BTYR385

220472

PDB entries from 2024-05-29

PDB statisticsPDBj update infoContact PDBjnumon