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1LT7

Oxidized Homo sapiens betaine-homocysteine S-methyltransferase in complex with four Sm(III) ions

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006479biological_processprotein methylation
A0006577biological_processamino-acid betaine metabolic process
A0006579biological_processamino-acid betaine catabolic process
A0008168molecular_functionmethyltransferase activity
A0008172molecular_functionS-methyltransferase activity
A0008270molecular_functionzinc ion binding
A0009086biological_processmethionine biosynthetic process
A0032259biological_processmethylation
A0046500biological_processS-adenosylmethionine metabolic process
A0046872molecular_functionmetal ion binding
A0047150molecular_functionbetaine-homocysteine S-methyltransferase activity
A0050666biological_processregulation of homocysteine metabolic process
A0070062cellular_componentextracellular exosome
A0071266biological_process'de novo' L-methionine biosynthetic process
A0071267biological_processL-methionine salvage
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006479biological_processprotein methylation
B0006577biological_processamino-acid betaine metabolic process
B0006579biological_processamino-acid betaine catabolic process
B0008168molecular_functionmethyltransferase activity
B0008172molecular_functionS-methyltransferase activity
B0008270molecular_functionzinc ion binding
B0009086biological_processmethionine biosynthetic process
B0032259biological_processmethylation
B0046500biological_processS-adenosylmethionine metabolic process
B0046872molecular_functionmetal ion binding
B0047150molecular_functionbetaine-homocysteine S-methyltransferase activity
B0050666biological_processregulation of homocysteine metabolic process
B0070062cellular_componentextracellular exosome
B0071266biological_process'de novo' L-methionine biosynthetic process
B0071267biological_processL-methionine salvage
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SM A 501
ChainResidue
ACIT601
AHOH618
AHOH646

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SM B 502
ChainResidue
AHOH694
BHOH702

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SM A 503
ChainResidue
AHOH749

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SM B 504
ChainResidue
BCIT602

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CIT A 601
ChainResidue
AARG356
ASM501
AHOH615
AHOH641
AHOH646
BTYR363
BLYS369
AHIS252
ALYS283

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CIT B 602
ChainResidue
AGLY360
APRO362
ATYR363
BASP220
BHIS252
BARG356
BSM504
BHOH606
BHOH639

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00333, ECO:0000269|PubMed:12220488, ECO:0007744|PDB:1LT8
ChainResidueDetails
ACYS217
ACYS299
ACYS300
BCYS217
BCYS299
BCYS300

site_idSWS_FT_FI2
Number of Residues12
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O35490
ChainResidueDetails
ALYS40
BLYS241
BLYS340
BLYS377
ALYS93
ALYS232
ALYS241
ALYS340
ALYS377
BLYS40
BLYS93
BLYS232

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O09171
ChainResidueDetails
ASER330
BSER330

223790

PDB entries from 2024-08-14

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