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3LAD

REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004148molecular_functiondihydrolipoyl dehydrogenase activity
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0050660molecular_functionflavin adenine dinucleotide binding
B0004148molecular_functiondihydrolipoyl dehydrogenase activity
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD A 480
ChainResidue
AGLY10
ATHR47
ACYS48
AGLY52
ACYS53
ASER56
ALYS57
AGLY119
AHIS120
AGLY121
AALA149
AGLY12
ASER150
AGLY151
AILE191
AARG278
ALEU285
AGLY317
AASP318
ALEU325
AALA326
AHIS327
APRO13
ATYR357
AHOH582
BHIS450
AGLY14
AILE32
AGLU33
ALYS34
ATYR35
AGLY46

site_idAC2
Number of Residues33
DetailsBINDING SITE FOR RESIDUE FAD B 480
ChainResidue
AHIS450
APRO451
BILE9
BGLY10
BGLY12
BPRO13
BGLY14
BILE32
BGLU33
BLYS34
BTYR35
BGLY46
BTHR47
BCYS48
BGLY52
BCYS53
BLYS57
BGLY119
BHIS120
BGLY121
BALA149
BSER150
BGLY151
BSER152
BILE191
BARG278
BGLY317
BASP318
BMET324
BLEU325
BALA326
BHIS327
BHOH704

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCLnvGCIP
ChainResidueDetails
AGLY45-PRO55

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS450
BHIS450

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:1880807
ChainResidueDetails
AGLU33
ALYS57
AASP318
AALA326
BGLU33
BLYS57
BASP318
BALA326

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY121
BALA275
AGLY187
AGLU210
AVAL244
AALA275
BGLY121
BGLY187
BGLU210
BVAL244

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
AGLU455
AHIS450

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BGLU455
BHIS450

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS48
ACYS53

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BCYS48
BCYS53

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PDB entries from 2024-07-10

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