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1Q7C

The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment

Functional Information from GO Data
ChainGOidnamespacecontents
A0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0008610biological_processlipid biosynthetic process
A0009102biological_processbiotin biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0030497biological_processfatty acid elongation
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0008610biological_processlipid biosynthetic process
B0009102biological_processbiotin biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0030497biological_processfatty acid elongation
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE NDP A 1901
ChainResidue
AGLY12
AGLY88
AILE89
AARG91
AHOH1011
ASER14
AARG15
AALA36
ATHR37
ALEU58
AASN59
AVAL60
AALA87

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NDP B 2901
ChainResidue
BSER14
BALA36
BTHR37
BLEU58
BASN59
BVAL60
BALA87
BGLY88
BILE89
BARG91
BHOH2011

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15016358","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q7B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q7C","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15016358","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q7B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15016358","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ALYS155
ASER138
APHE151
AASN110

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
BLYS155
BSER138
BPHE151
BASN110

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ALYS155
AGLN148

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
BLYS155
BGLN148

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ALYS155
APHE151

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
BLYS155
BPHE151

243083

PDB entries from 2025-10-15

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