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1I1N

HUMAN PROTEIN L-ISOASPARTATE O-METHYLTRANSFERASE WITH S-ADENOSYL HOMOCYSTEINE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004719molecular_functionprotein-L-isoaspartate (D-aspartate) O-methyltransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006479biological_processprotein methylation
A0008168molecular_functionmethyltransferase activity
A0016740molecular_functiontransferase activity
A0030091biological_processprotein repair
A0032259biological_processmethylation
A0036211biological_processprotein modification process
A0045296molecular_functioncadherin binding
A0070062cellular_componentextracellular exosome
A1903561cellular_componentextracellular vesicle
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE SAH A 1300
ChainResidue
AALA56
AASP109
AHIS110
AILE111
ALEU114
AGLY140
AASP141
AGLY142
AARG143
AGLY158
AVAL213
ATHR57
APRO214
ALEU215
ATHR216
AGLN221
AHOH307
AHOH308
AHOH316
AILE58
ASER59
AHIS64
AGLY85
ASER86
AGLY87
ASER88

Functional Information from PROSITE/UniProt
site_idPS01279
Number of Residues16
DetailsPCMT Protein-L-isoaspartate(D-aspartate) O-methyltransferase signature. GDGrmGYaeeAPYDaI
ChainResidueDetails
AGLY140-ILE155

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"Q27869","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11792715","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11847284","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1I1N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KR5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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