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2OFP

Crystal structure of Escherichia coli ketopantoate reductase in a ternary complex with NADP+ and pantoate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0008677molecular_function2-dehydropantoate 2-reductase activity
A0015940biological_processpantothenate biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0050661molecular_functionNADP binding
B0005737cellular_componentcytoplasm
B0008677molecular_function2-dehydropantoate 2-reductase activity
B0015940biological_processpantothenate biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 801
ChainResidue
BALA171
BLEU227
BHOH946

site_idAC2
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAP A 304
ChainResidue
ALEU30
AARG31
ATHR70
ALEU71
ALYS72
AGLN75
AALA79
AHIS97
AASN98
ATHR118
AHIS120
AALA121
AALA122
AGLU256
AHOH712
AHOH713
AHOH768
AHOH769
AHOH785
AHOH791
AHOH796
AHOH802
AHOH846
AHOH868
AHOH876
ALEU6
AGLY7
AGLY9
AALA10
ALEU11
ATRP29

site_idAC3
Number of Residues37
DetailsBINDING SITE FOR RESIDUE NAP B 802
ChainResidue
BLEU6
BGLY7
BCYS8
BGLY9
BALA10
BLEU11
BTRP29
BLEU30
BARG31
BTHR70
BLEU71
BLYS72
BGLN75
BHIS97
BASN98
BTHR118
BHIS120
BALA121
BALA122
BASN241
BSER244
BARG253
BGLU256
BPAF601
BHOH812
BHOH834
BHOH839
BHOH879
BHOH885
BHOH886
BHOH893
BHOH913
BHOH914
BHOH919
BHOH941
BHOH988
BHOH999

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PAF B 601
ChainResidue
BASN98
BLYS176
BASN180
BILE183
BASN184
BASN194
BASN241
BSER243
BSER244
BNAP802

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PAF A 602
ChainResidue
AASN98
AASN180
AASN184
AASN194
AVAL234
ASER243
ASER244
AHOH838
AHOH849
AHOH853

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DIO A 701
ChainResidue
AASP258
ATYR259
AARG266
BASN127

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DIO A 702
ChainResidue
BASN127
AGLY262
AARG266
AARG269
AHOH731

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DIO B 703
ChainResidue
AASP229
AGLN233
BLYS21
BGLU43
BASP45
BSER47
BHOH869

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DIO B 704
ChainResidue
BALA55
BASP57
BTRP190
BGLU203
BARG280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11123955","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15966718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17229734","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17229734","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 721
ChainResidueDetails
ALYS176proton acceptor, proton donor

site_idMCSA2
Number of Residues1
DetailsM-CSA 721
ChainResidueDetails
BLYS176proton acceptor, proton donor

246031

PDB entries from 2025-12-10

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