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4M3P

Betaine-Homocysteine S-Methyltransferase from Homo sapiens complexed with Homocysteine

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
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006479biological_processprotein methylation
C0006577biological_processamino-acid betaine metabolic process
C0006579biological_processamino-acid betaine catabolic process
C0008168molecular_functionmethyltransferase activity
C0008172molecular_functionS-methyltransferase activity
C0008270molecular_functionzinc ion binding
C0009086biological_processmethionine biosynthetic process
C0032259biological_processmethylation
C0046500biological_processS-adenosylmethionine metabolic process
C0046872molecular_functionmetal ion binding
C0047150molecular_functionbetaine-homocysteine S-methyltransferase activity
C0050666biological_processregulation of homocysteine metabolic process
C0070062cellular_componentextracellular exosome
C0071266biological_process'de novo' L-methionine biosynthetic process
C0071267biological_processL-methionine salvage
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006479biological_processprotein methylation
D0006577biological_processamino-acid betaine metabolic process
D0006579biological_processamino-acid betaine catabolic process
D0008168molecular_functionmethyltransferase activity
D0008172molecular_functionS-methyltransferase activity
D0008270molecular_functionzinc ion binding
D0009086biological_processmethionine biosynthetic process
D0032259biological_processmethylation
D0046500biological_processS-adenosylmethionine metabolic process
D0046872molecular_functionmetal ion binding
D0047150molecular_functionbetaine-homocysteine S-methyltransferase activity
D0050666biological_processregulation of homocysteine metabolic process
D0070062cellular_componentextracellular exosome
D0071266biological_process'de novo' L-methionine biosynthetic process
D0071267biological_processL-methionine salvage
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 701
ChainResidue
ACYS217
ACYS299
ACYS300
AHCS703

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K A 702
ChainResidue
AHOH825
AHOH945
AASP26
AGLY27
AGLN72
AGLN247
AGLY298

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HCS A 703
ChainResidue
AGLY27
APHE29
AVAL30
AGLN72
AGLU159
ATYR160
ACYS299
AZN701
AHOH808
AHOH825
AHOH928

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SRT B 501
ChainResidue
AGLU54
AARG57
BARG57
BARG61
BHOH617
BHOH626
BHOH717
CLYS150
CLYS151
CASN152
CHOH626
CHOH780

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 502
ChainResidue
BCYS217
BCYS299
BCYS300
BHCS504

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K B 503
ChainResidue
BASP26
BGLY27
BGLN72
BGLN247
BGLY298
BHOH701
BHOH737

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HCS B 504
ChainResidue
BGLY27
BGLY28
BPHE29
BVAL30
BGLN72
BGLU159
BTYR160
BCYS299
BZN502
BHOH642
BHOH701

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 501
ChainResidue
CCYS217
CCYS299
CCYS300
CHCS503

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K C 502
ChainResidue
CASP26
CGLY27
CGLN72
CGLN247
CGLY298
CHOH634
CHOH658

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HCS C 503
ChainResidue
CGLY27
CGLY28
CPHE29
CVAL30
CGLN72
CGLU159
CCYS299
CZN501
CHOH628
CHOH658
CHOH759

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SRT D 501
ChainResidue
ALYS150
ALYS151
AASN152
AHOH822
AHOH877
AHOH881
DARG57
DARG61
DHOH611
DHOH625

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 502
ChainResidue
DCYS217
DCYS299
DCYS300
DHCS504

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K D 503
ChainResidue
DASP26
DGLY27
DGLN72
DGLN247
DGLY298
DHOH684

site_idBC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HCS D 504
ChainResidue
DGLY28
DPHE29
DVAL30
DGLN72
DGLU159
DTYR160
DCYS299
DZN502
DHOH622
DHOH684
DGLY27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00333, ECO:0000269|PubMed:12220488, ECO:0007744|PDB:1LT8
ChainResidueDetails
ACYS217
ACYS299
ACYS300
BCYS217
BCYS299
BCYS300
CCYS217
CCYS299
CCYS300
DCYS217
DCYS299
DCYS300

site_idSWS_FT_FI2
Number of Residues24
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O35490
ChainResidueDetails
ALYS40
ALYS93
ALYS232
ALYS241
ALYS340
ALYS377
BLYS40
BLYS93
BLYS232
BLYS241
BLYS340
BLYS377
CLYS40
CLYS93
CLYS232
CLYS241
CLYS340
CLYS377
DLYS40
DLYS93
DLYS232
DLYS241
DLYS340
DLYS377

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O09171
ChainResidueDetails
ASER330
BSER330
CSER330
DSER330

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PDB entries from 2024-06-12

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