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1LVL

THE REFINED STRUCTURE OF PSEUDOMONAS PUTIDA LIPOAMIDE DEHYDROGENASE COMPLEXED WITH NAD+ AT 2.45 ANGSTROMS RESOLUTION

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
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE FAD A 459
ChainResidue
AILE11
ACYS48
ALYS52
AGLY116
ATRP117
AALA118
AALA141
ATHR142
AGLY143
ATYR181
AARG266
AGLY12
AARG269
AASP305
ALEU312
AALA313
AHIS314
AHIS437
APRO438
AHOH505
AGLY16
AGLU35
AGLY36
AGLY41
ATHR42
ACYS43
AGLY47

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAD A 460
ChainResidue
AVAL177
AGLY178
ATYR181
AILE182
AVAL200
AGLU201
AALA202
AVAL235
AALA263
AVAL264
AGLY265
AARG266
AGLU309
AMET311
AHOH461
AHOH470
AHOH508
AHOH583

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCLniGCIP
ChainResidueDetails
AGLY40-PRO50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AHIS437

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:1325638
ChainResidueDetails
AGLU35
AASP305
AMET311
AALA313
ALYS52
AALA118
AALA141
AGLY178
ATYR181
AGLU201
AVAL235
AALA263

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
AHIS437
AGLU442

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS48
ACYS43

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PDB entries from 2024-07-24

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