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2EX4

Crystal Structure of Human methyltransferase AD-003 in complex with S-adenosyl-L-homocysteine

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006338biological_processchromatin remodeling
A0006480biological_processN-terminal protein amino acid methylation
A0007051biological_processspindle organization
A0007059biological_processchromosome segregation
A0008168molecular_functionmethyltransferase activity
A0008276molecular_functionprotein methyltransferase activity
A0018013biological_processN-terminal peptidyl-glycine methylation
A0018016biological_processN-terminal peptidyl-proline dimethylation
A0032259biological_processmethylation
A0035572biological_processN-terminal peptidyl-serine dimethylation
A0035573biological_processN-terminal peptidyl-serine trimethylation
A0042054molecular_functionhistone methyltransferase activity
A0071885molecular_functionN-terminal protein N-methyltransferase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006338biological_processchromatin remodeling
B0006480biological_processN-terminal protein amino acid methylation
B0007051biological_processspindle organization
B0007059biological_processchromosome segregation
B0008168molecular_functionmethyltransferase activity
B0008276molecular_functionprotein methyltransferase activity
B0018013biological_processN-terminal peptidyl-glycine methylation
B0018016biological_processN-terminal peptidyl-proline dimethylation
B0032259biological_processmethylation
B0035572biological_processN-terminal peptidyl-serine dimethylation
B0035573biological_processN-terminal peptidyl-serine trimethylation
B0042054molecular_functionhistone methyltransferase activity
B0071885molecular_functionN-terminal protein N-methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SAH A 1401
ChainResidue
ATRP20
APHE97
ACYS118
AGLY119
ALEU120
AGLN121
AGLN136
ATRP137
AVAL138
AHIS141
AHOH1404
AMET30
AHOH1408
AHOH1410
AGLY70
AGLY72
AARG75
AILE76
AASP92
AILE93
ATHR94

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE SAH B 1402
ChainResidue
BTRP20
BMET30
BGLY70
BGLY72
BARG75
BILE76
BASP92
BILE93
BTHR94
BPHE97
BGLY119
BLEU120
BGLN121
BGLN136
BTRP137
BVAL138
BHIS141
BHOH1404
BHOH1409
BHOH1411

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:26543159, ECO:0000269|PubMed:26543161, ECO:0007744|PDB:2EX4, ECO:0007744|PDB:5CVD, ECO:0007744|PDB:5CVE, ECO:0007744|PDB:5E1D, ECO:0007744|PDB:5E1M, ECO:0007744|PDB:5E1O, ECO:0007744|PDB:5E2A, ECO:0007744|PDB:5E2B
ChainResidueDetails
AGLY70
BGLN136
AARG75
AASP92
ALEU120
AGLN136
BGLY70
BARG75
BASP92
BLEU120

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylthreonine; in N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed => ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
ATHR2
BTHR2

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1or8
ChainResidueDetails
AGLN136
AGLN145

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1or8
ChainResidueDetails
BGLN136
BGLN145

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1or8
ChainResidueDetails
AGLY140

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1or8
ChainResidueDetails
BGLY140

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PDB entries from 2024-07-24

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