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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
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q27869
ChainResidueDetails
AALA60

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:11792715, ECO:0000269|PubMed:11847284, ECO:0007744|PDB:1I1N, ECO:0007744|PDB:1KR5
ChainResidueDetails
ATHR57
AALA65
AGLY89
AHIS110
AGLY142
AASP217
ATRP222

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:2684970
ChainResidueDetails
ATRP2

218853

PDB entries from 2024-04-24

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