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5L46

Crystal structure of human dimethylglycine-dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006579biological_processamino-acid betaine catabolic process
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0019695biological_processcholine metabolic process
A0042426biological_processcholine catabolic process
A0047865molecular_functiondimethylglycine dehydrogenase activity
B0003723molecular_functionRNA binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006579biological_processamino-acid betaine catabolic process
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0019695biological_processcholine metabolic process
B0042426biological_processcholine catabolic process
B0047865molecular_functiondimethylglycine dehydrogenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues33
Detailsbinding site for residue FAD A 901
ChainResidue
AILE55
AGLY87
ASER88
ATHR89
AHIS91
AALA93
ALEU95
APRO218
AVAL219
AALA247
AALA248
AGLY56
AGLY249
ATRP251
AVAL255
AHIS270
ATYR272
AGLY370
APRO371
AILE372
APHE397
AGLY398
AGLY57
ATYR399
AGLY400
AILE401
AILE402
AGLY58
ACYS59
AVAL60
ALEU79
AGLU80
ALYS81

site_idAC2
Number of Residues31
Detailsbinding site for Di-peptide FAD B 901 and HIS B 64
ChainResidue
BILE55
BGLY56
BGLY57
BGLY58
BCYS59
BVAL60
BLEU79
BGLU80
BLYS81
BGLY87
BSER88
BTHR89
BTRP90
BALA92
BALA93
BGLY94
BLEU95
BVAL219
BALA248
BGLY249
BTRP251
BHIS270
BTYR272
BVAL368
BPRO371
BILE372
BPHE397
BTYR399
BGLY400
BILE401
BILE402

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:27486859, ECO:0007744|PDB:5L46
ChainResidueDetails
BVAL219
BPHE397
ACYS59
AGLU80
AGLY87
AVAL219
APHE397
BCYS59
BGLU80
BGLY87

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q63342
ChainResidueDetails
ATYR676
AGLU683
ATYR744
BTRP251
BGLU580
BTYR676
BGLU683
BTYR744
ATRP251
AGLU580

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Tele-8alpha-FAD histidine => ECO:0000269|PubMed:27486859, ECO:0007744|PDB:5L46
ChainResidueDetails
AHIS91
BHIS91

site_idSWS_FT_FI4
Number of Residues12
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DBT9
ChainResidueDetails
ALYS360
ALYS764
BLYS114
BLYS168
BLYS223
BLYS335
BLYS360
BLYS764
ALYS114
ALYS168
ALYS223
ALYS335

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DBT9
ChainResidueDetails
ALYS523
ALYS655
BLYS148
BLYS434
BLYS523
BLYS655
ALYS148
ALYS434

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9DBT9
ChainResidueDetails
ALYS317
ALYS319
ALYS795
BLYS317
BLYS319
BLYS795

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PDB entries from 2024-06-12

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