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5YF2

Crystal structure of CARNMT1 bound to anserine and SAH

Functional Information from GO Data
ChainGOidnamespacecontents
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
B0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue SAH A 501
ChainResidue
AARG167
AASP295
APHE296
ACYS312
APHE313
APHE314
ATHR317
ATYR324
ATYR386
A8V3502
AHOH604
ATYR181
AGLY208
AASN228
AGLU229
ATRP230
ASER231
AMET234
AGLY294

site_idAC2
Number of Residues8
Detailsbinding site for residue 8V3 A 502
ChainResidue
APHE313
AASP316
APRO343
ALEU345
ATYR386
ATYR398
ASAH501
AHOH609

site_idAC3
Number of Residues1
Detailsbinding site for residue CA A 503
ChainResidue
AASP363

site_idAC4
Number of Residues1
Detailsbinding site for residue P6G A 504
ChainResidue
AGLU399

site_idAC5
Number of Residues17
Detailsbinding site for residue SAH B 501
ChainResidue
BARG167
BTYR181
BGLY208
BASN228
BGLU229
BTRP230
BSER231
BMET234
BASP295
BPHE296
BCYS312
BPHE313
BPHE314
BTHR317
BTYR324
BTYR386
BHOH638

site_idAC6
Number of Residues6
Detailsbinding site for residue 8V3 B 502
ChainResidue
BPHE313
BASP316
BPRO343
BTYR386
BTYR396
BTYR398

site_idAC7
Number of Residues5
Detailsbinding site for residue CA B 503
ChainResidue
BGLU88
BASP110
BHOH668
BHOH705
BHOH706

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:29463897, ECO:0007744|PDB:5YF0
ChainResidueDetails
AGLN164
BARG167
BGLY208
BGLU229
BASP295
BPHE296
BCYS312
BTYR324
AARG167
AGLY208
AGLU229
AASP295
APHE296
ACYS312
ATYR324
BGLN164

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:29463897, ECO:0007744|PDB:5YF1
ChainResidueDetails
AASP316
AHIS347
ATYR398
BASP316
BHIS347
BTYR398

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PDB entries from 2024-07-10

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