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3GQV

Lovastatin polyketide enoyl reductase (LovC) mutant K54S with bound NADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
A0008152biological_processmetabolic process
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 Residues38
DetailsBINDING SITE FOR RESIDUE NAP A 372
ChainResidue
APRO50
AASN200
ATYR215
ACYS238
AILE239
AASN241
ALEU262
AASN263
ATHR280
AGLY282
ALEU351
ASER51
ASER352
AHOH377
AHOH383
AHOH391
AHOH395
AHOH397
AHOH404
AGOL410
AHOH412
AHOH414
ATHR139
AHOH431
AHOH432
AHOH471
AHOH484
AHOH488
AHOH491
AHOH495
AHOH531
AHOH533
ASER174
ATHR175
AALA176
ATHR177
ACYS196
ASER197

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 410
ChainResidue
APRO50
AILE239
ANAP372

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 373
ChainResidue
AGLY87
AASP88
AARG89
AILE121

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

218853

PDB entries from 2024-04-24

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