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3B70

Crystal structure of Aspergillus terreus trans-acting lovastatin polyketide enoyl reductase (LovC) with bound NADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
A0016218molecular_functionpolyketide synthase activity
A0016491molecular_functionoxidoreductase activity
A0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
A0016740molecular_functiontransferase activity
A0030639biological_processpolyketide biosynthetic process
A0050637molecular_functionlovastatin nonaketide synthase activity
A0070402molecular_functionNADPH binding
A0140735biological_processlovastatin biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NAP A 372
ChainResidue
APRO50
ASER197
AHIS199
AASN200
ATYR215
ACYS238
AILE239
AASN241
ALEU262
AASN263
ATHR280
ASER51
AGLY282
ASER352
AGLY353
AGOL373
AHOH383
AHOH391
AHOH395
AHOH397
AHOH404
AHOH412
ALYS54
AHOH414
AHOH435
AHOH436
AHOH492
ATHR139
ASER174
ATHR175
AALA176
ATHR177
ACYS196

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 373
ChainResidue
APRO50
AILE239
ANAP372

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:22733743
ChainResidueDetails
ASER51
ASER174
ASER197
ATYR215
ALEU262
ATHR280
ALEU351

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AALA135
AGLY282

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qlh
ChainResidueDetails
ASER51
ALYS54

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PDB entries from 2024-11-06

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