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1KR5

Crystal structure of human L-isoaspartyl methyltransferase

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 Residues23
DetailsBINDING SITE FOR RESIDUE SAH A 300
ChainResidue
AALA56
AASP109
AHIS110
ALEU114
AGLY140
AASP141
AGLY142
AARG143
AGLY158
APRO214
ALEU215
ATHR57
ATHR216
AGLN221
AHOH301
AHOH304
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

243083

PDB entries from 2025-10-15

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