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1XCJ

Guanidinoacetate methyltransferase containing S-adenosylhomocysteine and guanidinoacetate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006601biological_processcreatine biosynthetic process
A0007283biological_processspermatogenesis
A0008168molecular_functionmethyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0009887biological_processanimal organ morphogenesis
A0016740molecular_functiontransferase activity
A0019702molecular_functionprotein arginine N5-methyltransferase activity
A0030731molecular_functionguanidinoacetate N-methyltransferase activity
A0032259biological_processmethylation
A0040014biological_processregulation of multicellular organism growth
A0042802molecular_functionidentical protein binding
A0046498biological_processS-adenosylhomocysteine metabolic process
A0046500biological_processS-adenosylmethionine metabolic process
A1990402biological_processembryonic liver development
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE SAH A 236
ChainResidue
ATRP19
AILE72
AALA73
AGLU89
ACYS90
AASN91
AVAL94
AGLY114
ALEU115
ATRP116
AGLU117
AVAL40
AASP134
ATHR135
ATYR136
ALEU138
AHOH1002
AMET41
AMET49
AGLY67
APHE68
AGLY69
AMET70
AALA71

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NMG A 237
ChainResidue
AVAL40
AMET41
AGLU45
AASP134
ATHR135
ACYS168
AASN169
ALEU170
ATHR171
AHOH1009
AHOH1052

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AARG20
AHIS50
AGLY69
AGLU117
ATHR135

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00892, ECO:0000269|PubMed:15533043, ECO:0007744|PDB:1XCJ
ChainResidueDetails
AGLU42
ATHR46

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15533043, ECO:0007744|PDB:1XCJ
ChainResidueDetails
ATHR171

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:Q14353
ChainResidueDetails
ASER2

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
APRO7

218853

PDB entries from 2024-04-24

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