Structure of PDB 7qlq Chain AAA Binding Site BS02

Receptor Information
>7qlq Chain AAA (length=383) Species: 511145 (Escherichia coli str. K-12 substr. MG1655) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ANRMILNETAWFGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVT
DKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLIAIGGGSPQD
TCKAIGIISNNPEFADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTIGY
VITDEEKRRKFVCVDPHDIPQVAFIDADMMDGMPPALKAATGVDALTHAI
EGYITRGAWALTDALHIKAIEIIAGALRGSVAGDKDAGEEMALGQYVAGM
GFSNVGVGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRD
IARVMGVKVEGMSLEEARNAAVEAVFALNRDVGIPPHLRDVGVRKEDIPA
LAQAALDDVCTGGNPREATLEDIVELYHTAWTS
Ligand information
Ligand IDAPR
InChIInChI=1S/C15H23N5O14P2/c16-12-7-13(18-3-17-12)20(4-19-7)14-10(23)8(21)5(32-14)1-30-35(26,27)34-36(28,29)31-2-6-9(22)11(24)15(25)33-6/h3-6,8-11,14-15,21-25H,1-2H2,(H,26,27)(H,28,29)(H2,16,17,18)/t5-,6-,8-,9-,10-,11-,14-,15-/m1/s1
InChIKeySRNWOUGRCWSEMX-KEOHHSTQSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(OCC3OC(n1c2ncnc(N)c2nc1)C(O)C3O)OP(=O)(O)OCC4OC(O)C(O)C4O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)O)O)O)O)O)N
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)O)O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]4O[CH](O)[CH](O)[CH]4O)[CH](O)[CH]3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P@@](O)(=O)OC[C@H]4O[C@@H](O)[C@H](O)[C@@H]4O)[C@@H](O)[C@H]3O
FormulaC15 H23 N5 O14 P2
NameADENOSINE-5-DIPHOSPHORIBOSE
ChEMBLCHEMBL1231026
DrugBank
ZINCZINC000017654550
PDB chain7qlq Chain AAA Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7qlq Crystal structures and kinetic studies of a laboratory evolved aldehyde reductase explain the dramatic shift of its new substrate specificity.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		D39 T41 L42 G97 G98 S99 T140 T141 T144 K162 G184 M185 L189 H277
Binding residue
(residue number reindexed from 1)		D37 T39 L40 G95 G96 S97 T138 T139 T142 K160 G182 M183 L187 H275
Annotation score3
Enzymatic activity
Enzyme Commision number 1.1.1.77: lactaldehyde reductase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004022 alcohol dehydrogenase (NAD+) activity
GO:0008198 ferrous iron binding
GO:0008912 lactaldehyde reductase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0052660 R-lactaldehyde reductase activity
GO:0052661 S-lactaldehyde reductase activity
Biological Process
GO:0006004 fucose metabolic process
GO:0019301 rhamnose catabolic process
GO:0019317 fucose catabolic process
GO:0042355 L-fucose catabolic process
GO:0042846 glycol catabolic process
GO:0051143 propanediol metabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7qlq, PDBe:7qlq, PDBj:7qlq
PDBsum7qlq
PubMed37261425
UniProtP0A9S1|FUCO_ECOLI Lactaldehyde reductase (Gene Name=fucO)

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