ID O76290_TRYBB Unreviewed; 268 AA.
AC O76290;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE SubName: Full=Pteridine reductase {ECO:0000313|EMBL:AAC23562.1};
GN Name=PTR1 {ECO:0000313|EMBL:AAC23562.1};
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702 {ECO:0000313|EMBL:AAC23562.1};
RN [1] {ECO:0000313|EMBL:AAC23562.1}
RP NUCLEOTIDE SEQUENCE.
RA Hiller R.R.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:2C7V}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NADP(+), AND ACTIVE
RP SITE.
RX PubMed=16968221; DOI=10.1111/j.1365-2958.2006.05332.x;
RA Dawson A., Gibellini F., Sienkiewicz N., Tulloch L.B., Fyfe P.K.,
RA McLuskey K., Fairlamb A.H., Hunter W.N.;
RT "Structure and reactivity of Trypanosoma brucei pteridine reductase:
RT inhibition by the archetypal antifolate methotrexate.";
RL Mol. Microbiol. 61:1457-1468(2006).
RN [3] {ECO:0007829|PDB:2WD7, ECO:0007829|PDB:2WD8}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX PubMed=19527033; DOI=10.1021/jm900414x;
RA Mpamhanga C.P., Spinks D., Tulloch L.B., Shanks E.J., Robinson D.A.,
RA Collie I.T., Fairlamb A.H., Wyatt P.G., Frearson J.A., Hunter W.N.,
RA Gilbert I.H., Brenk R.;
RT "One scaffold, three binding modes: novel and selective pteridine reductase
RT 1 inhibitors derived from fragment hits discovered by virtual screening.";
RL J. Med. Chem. 52:4454-4465(2009).
RN [4] {ECO:0007829|PDB:2X9G, ECO:0007829|PDB:2X9N}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX PubMed=21123874; DOI=10.1107/s0907444910040886;
RA Dawson A., Tulloch L.B., Barrack K.L., Hunter W.N.;
RT "High-resolution structures of Trypanosoma brucei pteridine reductase
RT ligand complexes inform on the placement of new molecular entities in the
RT active site of a potential drug target.";
RL Acta Crystallogr. D 66:1334-1340(2010).
RN [5] {ECO:0007829|PDB:2VZ0}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX PubMed=19748480; DOI=10.1016/j.ab.2009.09.003;
RA Shanks E.J., Ong H.B., Robinson D.A., Thompson S., Sienkiewicz N.,
RA Fairlamb A.H., Frearson J.A.;
RT "Development and validation of a cytochrome c-coupled assay for pteridine
RT reductase 1 and dihydrofolate reductase.";
RL Anal. Biochem. 396:194-203(2010).
RN [6] {ECO:0007829|PDB:3BMC, ECO:0007829|PDB:3BMN}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX PubMed=19916554; DOI=10.1021/jm901059x;
RA Tulloch L.B., Martini V.P., Iulek J., Huggan J.K., Lee J.H., Gibson C.L.,
RA Smith T.K., Suckling C.J., Hunter W.N.;
RT "Structure-based design of pteridine reductase inhibitors targeting African
RT sleeping sickness and the leishmaniases.";
RL J. Med. Chem. 53:221-229(2010).
RN [7] {ECO:0007829|PDB:4CL8, ECO:0007829|PDB:4CLD}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX PubMed=25007262; DOI=10.1021/jm500483b;
RA Khalaf A.I., Huggan J.K., Suckling C.J., Gibson C.L., Stewart K.,
RA Giordani F., Barrett M.P., Wong P.E., Barrack K.L., Hunter W.N.;
RT "Structure-based design and synthesis of antiparasitic pyrrolopyrimidines
RT targeting pteridine reductase 1.";
RL J. Med. Chem. 57:6479-6494(2014).
RN [8] {ECO:0007829|PDB:5JCJ, ECO:0007829|PDB:5JCX}
RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX PubMed=27411733; DOI=10.1021/acs.jmedchem.6b00698;
RA Borsari C., Luciani R., Pozzi C., Poehner I., Henrich S., Trande M.,
RA Cordeiro-da-Silva A., Santarem N., Baptista C., Tait A., Di Pisa F.,
RA Dello Iacono L., Landi G., Gul S., Wolf M., Kuzikov M., Ellinger B.,
RA Reinshagen J., Witt G., Gribbon P., Kohler M., Keminer O., Behrens B.,
RA Costantino L., Tejera Nevado P., Bifeld E., Eick J., Clos J., Torrado J.,
RA Jimenez-Anton M.D., Corral M.J., Alunda J.M., Pellati F., Wade R.C.,
RA Ferrari S., Mangani S., Costi M.P.;
RT "Profiling of Flavonol Derivatives for the Development of
RT Antitrypanosomatidic Drugs.";
RL J. Med. Chem. 59:7598-7616(2016).
RN [9] {ECO:0007829|PDB:2YHU, ECO:0007829|PDB:4WCD}
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEX WITH NADP(+) AND NADPH.
RX PubMed=28983525; DOI=10.1021/acsomega.7b00473;
RA Linciano P., Dawson A., Pohner I., Costa D.M., Sa M.S.,
RA Cordeiro-da-Silva A., Luciani R., Gul S., Witt G., Ellinger B., Kuzikov M.,
RA Gribbon P., Reinshagen J., Wolf M., Behrens B., Hannaert V.,
RA Michels P.A.M., Nerini E., Pozzi C., di Pisa F., Landi G., Santarem N.,
RA Ferrari S., Saxena P., Lazzari S., Cannazza G., Freitas-Junior L.H.,
RA Moraes C.B., Pascoalino B.S., Alcantara L.M., Bertolacini C.P., Fontana V.,
RA Wittig U., Muller W., Wade R.C., Hunter W.N., Mangani S., Costantino L.,
RA Costi M.P.;
RT "Exploiting the 2-Amino-1,3,4-thiadiazole Scaffold To Inhibit
RT Trypanosoma brucei Pteridine Reductase in Support of Early-Stage
RT Drug Discovery.";
RL ACS Omega 2:5666-5683(2017).
RN [10] {ECO:0007829|PDB:5K6A}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX PubMed=28282886; DOI=10.3390/molecules22030426;
RA Di Pisa F., Landi G., Dello Iacono L., Pozzi C., Borsari C., Ferrari S.,
RA Santucci M., Santarem N., Cordeiro-da-Silva A., Moraes C.B.,
RA Alcantara L.M., Fontana V., Freitas-Junior L.H., Gul S., Kuzikov M.,
RA Behrens B., Pohner I., Wade R.C., Costi M.P., Mangani S.;
RT "Chroman-4-One Derivatives Targeting Pteridine Reductase 1 and Showing
RT Anti-Parasitic Activity. .";
RL Molecules 22:E426-E426(2017).
RN [11] {ECO:0007829|PDB:6HNC, ECO:0007829|PDB:6HNR}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX PubMed=31012301; DOI=10.1021/acsinfecdis.8b00358;
RA Landi G., Linciano P., Borsari C., Bertolacini C.P., Moraes C.B.,
RA Cordeiro-da-Silva A., Gul S., Witt G., Kuzikov M., Costi M.P., Pozzi C.,
RA Mangani S.;
RT "Structural Insights into the Development of Cycloguanil Derivatives as
RT Trypanosoma brucei Pteridine-Reductase-1 Inhibitors.";
RL ACS Infect. Dis. 5:1105-1114(2019).
RN [12] {ECO:0007829|PDB:6GCK, ECO:0007829|PDB:6GCL}
RP X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX PubMed=30908048; DOI=10.1021/acs.jmedchem.8b02021;
RA Linciano P., Pozzi C., Iacono L.D., di Pisa F., Landi G., Bonucci A.,
RA Gul S., Kuzikov M., Ellinger B., Witt G., Santarem N., Baptista C.,
RA Franco C., Moraes C.B., Muller W., Wittig U., Luciani R., Sesenna A.,
RA Quotadamo A., Ferrari S., Pohner I., Cordeiro-da-Silva A., Mangani S.,
RA Costantino L., Costi M.P.;
RT "Enhancement of Benzothiazoles as Pteridine Reductase-1 Inhibitors for the
RT Treatment of Trypanosomatidic Infections.";
RL J. Med. Chem. 62:3989-4012(2019).
RN [13] {ECO:0007829|PDB:6TBX}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX PubMed=32496217; DOI=10.1107/s2059798320004891;
RA Landi G., Linciano P., Tassone G., Costi M.P., Mangani S., Pozzi C.;
RT "High-resolution crystal structure of Trypanosoma brucei pteridine
RT reductase 1 in complex with an innovative tricyclic-based inhibitor.";
RL Acta Crystallogr. D Struct. Biol. 76:558-564(2020).
RN [14] {ECO:0007829|PDB:7OPJ}
RP X-RAY CRYSTALLOGRAPHY (1.34 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX PubMed=34209148; DOI=10.3390/ph14070636;
RA Tassone G., Landi G., Linciano P., Francesconi V., Tonelli M.,
RA Tagliazucchi L., Costi M.P., Mangani S., Pozzi C.;
RT "Evidence of Pyrimethamine and Cycloguanil Analogues as Dual Inhibitors of
RT Trypanosoma brucei Pteridine Reductase and Dihydrofolate Reductase. .";
RL Pharmaceuticals (Basel) 14:636-636(2021).
RN [15] {ECO:0007829|PDB:6RX0, ECO:0007829|PDB:6RX5}
RP X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX PubMed=35675511; DOI=10.1021/acs.jmedchem.2c00232;
RA Pohner I., Quotadamo A., Panecka-Hofman J., Luciani R., Santucci M.,
RA Linciano P., Landi G., Di Pisa F., Dello Iacono L., Pozzi C., Mangani S.,
RA Gul S., Witt G., Ellinger B., Kuzikov M., Santarem N.,
RA Cordeiro-da-Silva A., Costi M.P., Venturelli A., Wade R.C.;
RT "Multitarget, Selective Compound Design Yields Potent Inhibitors of a
RT Kinetoplastid Pteridine Reductase 1.";
RL J. Med. Chem. 65:9011-9033(2022).
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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DR EMBL; AF049903; AAC23562.1; -; mRNA.
DR PDB; 2C7V; X-ray; 2.20 A; A/B/C/D=1-268.
DR PDB; 2VZ0; X-ray; 1.90 A; A/B/C/D=1-268.
DR PDB; 2WD7; X-ray; 1.90 A; A/B/C/D=1-268.
DR PDB; 2WD8; X-ray; 2.10 A; A/B/C/D=1-268.
DR PDB; 2X9G; X-ray; 1.10 A; A/B/C/D=1-268.
DR PDB; 2X9N; X-ray; 1.15 A; A/B/C/D=1-268.
DR PDB; 2X9V; X-ray; 1.30 A; A/B/C/D=1-268.
DR PDB; 2YHU; X-ray; 2.01 A; A/B/C/D=1-268.
DR PDB; 3BMC; X-ray; 2.60 A; A/B/C/D=1-268.
DR PDB; 3BMN; X-ray; 1.98 A; A/B/C/D=1-268.
DR PDB; 3BMO; X-ray; 1.60 A; A/B/C/D=1-268.
DR PDB; 3BMQ; X-ray; 1.70 A; A/B/C/D=1-268.
DR PDB; 3GN1; X-ray; 2.00 A; A/B/C/D=1-268.
DR PDB; 3GN2; X-ray; 1.60 A; A/B/C/D=1-268.
DR PDB; 3MCV; X-ray; 1.70 A; A/B/C/D=1-268.
DR PDB; 4CL8; X-ray; 2.20 A; A/B/C/D=1-268.
DR PDB; 4CLD; X-ray; 1.77 A; A/B/C/D=1-268.
DR PDB; 4CLE; X-ray; 1.80 A; A/B/C/D=1-268.
DR PDB; 4CLH; X-ray; 1.85 A; A/B/C/D=1-268.
DR PDB; 4CLO; X-ray; 1.88 A; A/B/C/D=1-268.
DR PDB; 4CLR; X-ray; 1.75 A; A/B/C/D=1-268.
DR PDB; 4CLX; X-ray; 1.85 A; A/B/C/D=1-268.
DR PDB; 4CM1; X-ray; 1.90 A; A/B/C/D=1-268.
DR PDB; 4CM3; X-ray; 1.95 A; A/B/C/D=1-268.
DR PDB; 4CM4; X-ray; 1.81 A; A/B/C/D=1-268.
DR PDB; 4CM5; X-ray; 1.99 A; A/B/C/D=1-268.
DR PDB; 4CM6; X-ray; 1.70 A; A/B/C/D=1-268.
DR PDB; 4CM7; X-ray; 1.90 A; A/B/C/D=1-268.
DR PDB; 4CM8; X-ray; 1.90 A; A/B/C/D=1-268.
DR PDB; 4CM9; X-ray; 1.90 A; A/B/C/D=1-268.
DR PDB; 4CMA; X-ray; 1.85 A; A/B/C/D=1-268.
DR PDB; 4CMB; X-ray; 1.96 A; A/B/C/D=1-268.
DR PDB; 4CMC; X-ray; 1.85 A; A/B/C/D=1-268.
DR PDB; 4CME; X-ray; 1.85 A; A/B/C/D=1-268.
DR PDB; 4CMG; X-ray; 2.00 A; A/B/C/D=1-268.
DR PDB; 4CMI; X-ray; 1.90 A; A/B/C/D=1-268.
DR PDB; 4CMJ; X-ray; 2.20 A; A/B/C/D=1-268.
DR PDB; 4CMK; X-ray; 2.00 A; A/B/C/D=1-268.
DR PDB; 4WCD; X-ray; 1.68 A; A/B/C/D=1-268.
DR PDB; 4WCF; X-ray; 1.93 A; A/B/C/D=1-268.
DR PDB; 5IZC; X-ray; 1.92 A; A/B/C/D=1-268.
DR PDB; 5JCJ; X-ray; 1.76 A; A/B/C/D=1-268.
DR PDB; 5JCX; X-ray; 1.43 A; A/B/C/D=1-268.
DR PDB; 5JDC; X-ray; 1.78 A; A/B/C/D=1-268.
DR PDB; 5JDI; X-ray; 1.38 A; A/B/C/D=1-268.
DR PDB; 5K6A; X-ray; 1.70 A; A/B/C/D=1-268.
DR PDB; 6GCK; X-ray; 2.14 A; A/B/C/D=1-268.
DR PDB; 6GCL; X-ray; 1.95 A; A/B/C/D=1-268.
DR PDB; 6GCP; X-ray; 1.52 A; A/B/C/D=1-268.
DR PDB; 6GCQ; X-ray; 1.58 A; A/B/C/D=1-268.
DR PDB; 6GD0; X-ray; 1.74 A; A/B/C/D=1-268.
DR PDB; 6GD4; X-ray; 1.42 A; A/B/C/D=1-268.
DR PDB; 6GDO; X-ray; 1.78 A; A/B/C/D=1-268.
DR PDB; 6GDP; X-ray; 1.52 A; A/B/C/D=1-268.
DR PDB; 6GEX; X-ray; 1.78 A; A/B/C/D=1-268.
DR PDB; 6GEY; X-ray; 1.56 A; A/B/C/D=1-268.
DR PDB; 6HNC; X-ray; 1.50 A; A/B/C/D=1-268.
DR PDB; 6HNR; X-ray; 1.58 A; A/B/C/D=1-268.
DR PDB; 6HOW; X-ray; 1.92 A; A/B/C/D=1-268.
DR PDB; 6RX0; X-ray; 1.20 A; A/B/C/D=1-268.
DR PDB; 6RX5; X-ray; 1.42 A; A/B/C/D=1-268.
DR PDB; 6RX6; X-ray; 1.11 A; A/B/C/D=1-268.
DR PDB; 6TBX; X-ray; 1.30 A; A/B/C/D=1-268.
DR PDB; 7OPJ; X-ray; 1.34 A; A/B/C/D=1-268.
DR PDBsum; 2C7V; -.
DR PDBsum; 2VZ0; -.
DR PDBsum; 2WD7; -.
DR PDBsum; 2WD8; -.
DR PDBsum; 2X9G; -.
DR PDBsum; 2X9N; -.
DR PDBsum; 2X9V; -.
DR PDBsum; 2YHU; -.
DR PDBsum; 3BMC; -.
DR PDBsum; 3BMN; -.
DR PDBsum; 3BMO; -.
DR PDBsum; 3BMQ; -.
DR PDBsum; 3GN1; -.
DR PDBsum; 3GN2; -.
DR PDBsum; 3MCV; -.
DR PDBsum; 4CL8; -.
DR PDBsum; 4CLD; -.
DR PDBsum; 4CLE; -.
DR PDBsum; 4CLH; -.
DR PDBsum; 4CLO; -.
DR PDBsum; 4CLR; -.
DR PDBsum; 4CLX; -.
DR PDBsum; 4CM1; -.
DR PDBsum; 4CM3; -.
DR PDBsum; 4CM4; -.
DR PDBsum; 4CM5; -.
DR PDBsum; 4CM6; -.
DR PDBsum; 4CM7; -.
DR PDBsum; 4CM8; -.
DR PDBsum; 4CM9; -.
DR PDBsum; 4CMA; -.
DR PDBsum; 4CMB; -.
DR PDBsum; 4CMC; -.
DR PDBsum; 4CME; -.
DR PDBsum; 4CMG; -.
DR PDBsum; 4CMI; -.
DR PDBsum; 4CMJ; -.
DR PDBsum; 4CMK; -.
DR PDBsum; 4WCD; -.
DR PDBsum; 4WCF; -.
DR PDBsum; 5IZC; -.
DR PDBsum; 5JCJ; -.
DR PDBsum; 5JCX; -.
DR PDBsum; 5JDC; -.
DR PDBsum; 5JDI; -.
DR PDBsum; 5K6A; -.
DR PDBsum; 6GCK; -.
DR PDBsum; 6GCL; -.
DR PDBsum; 6GCP; -.
DR PDBsum; 6GCQ; -.
DR PDBsum; 6GD0; -.
DR PDBsum; 6GD4; -.
DR PDBsum; 6GDO; -.
DR PDBsum; 6GDP; -.
DR PDBsum; 6GEX; -.
DR PDBsum; 6GEY; -.
DR PDBsum; 6HNC; -.
DR PDBsum; 6HNR; -.
DR PDBsum; 6HOW; -.
DR AlphaFoldDB; O76290; -.
DR SMR; O76290; -.
DR BindingDB; O76290; -.
DR SABIO-RK; O76290; -.
DR EvolutionaryTrace; O76290; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0047040; F:pteridine reductase activity; IMP:CACAO.
DR CDD; cd05357; PR_SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR014058; Pteridine_reductase.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR NCBIfam; TIGR02685; pter_reduc_Leis; 1.
DR PANTHER; PTHR43639; OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870); 1.
DR PANTHER; PTHR43639:SF1; OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE_REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870); 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2C7V, ECO:0007829|PDB:2VZ0};
KW Nucleotide-binding {ECO:0007829|PDB:2VZ0, ECO:0007829|PDB:2WD7}.
FT ACT_SITE 161
FT /note="EMO_00070 proton relay,EMO_00114 hydrogen bond
FT donor,EMO_00113 hydrogen bond acceptor,EMO_00113 hydrogen
FT bond acceptor,EMO_00114 hydrogen bond donor,EMO_00114
FT hydrogen bond donor,EMO_00113 hydrogen bond
FT acceptor,EMO_00066 proton acceptor,EMO_00068 proton donor"
FT /evidence="ECO:0007829|PDB:2C7V"
FT ACT_SITE 174
FT /note="EMO_00070 proton relay,EMO_00114 hydrogen bond
FT donor,EMO_00113 hydrogen bond acceptor,EMO_00033
FT electrostatic stabiliser,EMO_00114 hydrogen bond
FT donor,EMO_00114 hydrogen bond donor,EMO_00068 proton
FT donor,EMO_00066 proton acceptor"
FT /evidence="ECO:0007829|PDB:2C7V"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR614058-1"
FT BINDING 13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:6GCQ"
FT BINDING 14
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:2VZ0, ECO:0007829|PDB:2WD7"
FT BINDING 14
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:2YHU"
FT BINDING 15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:2VZ0, ECO:0007829|PDB:2WD7"
FT BINDING 15
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:2YHU"
FT BINDING 35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:2VZ0, ECO:0007829|PDB:2WD7"
FT BINDING 35
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:2YHU"
FT BINDING 36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:2VZ0, ECO:0007829|PDB:2WD7"
FT BINDING 36
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:2YHU"
FT BINDING 37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:2VZ0, ECO:0007829|PDB:2WD7"
FT BINDING 37
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:2YHU"
FT BINDING 62
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:2VZ0, ECO:0007829|PDB:2WD7"
FT BINDING 62
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:2YHU"
FT BINDING 63
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:2VZ0, ECO:0007829|PDB:2WD7"
FT BINDING 63
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:2YHU"
FT BINDING 64
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:2WD7, ECO:0007829|PDB:2WD8"
FT BINDING 64
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:2YHU"
FT BINDING 93
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:2VZ0, ECO:0007829|PDB:2WD7"
FT BINDING 93
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:2YHU"
FT BINDING 95
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:2VZ0, ECO:0007829|PDB:2WD7"
FT BINDING 95
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:2YHU"
FT BINDING 126
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:6GEY"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR614058-2"
FT BINDING 174
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:2WD7, ECO:0007829|PDB:3BMC"
FT BINDING 174
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:2YHU"
FT BINDING 178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:2VZ0, ECO:0007829|PDB:2WD7"
FT BINDING 178
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:2YHU"
FT BINDING 205
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:4CLE, ECO:0007829|PDB:6HNC"
FT BINDING 207
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:2VZ0, ECO:0007829|PDB:2WD7"
FT BINDING 207
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:2YHU"
FT BINDING 208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:2VZ0, ECO:0007829|PDB:2WD7"
FT BINDING 208
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:2YHU"
FT SITE 14
FT /note="EMO_00114 hydrogen bond donor,EMO_00033
FT electrostatic stabiliser,EMO_00114 hydrogen bond
FT donor,EMO_00033 electrostatic stabiliser,EMO_00033
FT electrostatic stabiliser,EMO_00114 hydrogen bond
FT donor,EMO_00029 steric role"
FT /evidence="ECO:0007829|PDB:2C7V"
SQ SEQUENCE 268 AA; 28470 MW; 346C8257BDC9DD3D CRC64;
MEAPAAVVTG AAKRIGRAIA VKLHQTGYRV VIHYHNSAEA AVSLADELNK ERSNTAVVCQ
ADLTNSNVLP ASCEEIINSC FRAFGRCDVL VNNASAFYPT PLVQGDHEDN SNGKTVETQV
AELIGTNAIA PFLLTMSFAQ RQKGTNPNCT SSNLSIVNLC DAMVDQPCMA FSLYNMGKHA
LVGLTQSAAL ELAPYGIRVN GVAPGVSLLP VAMGEEEKDK WRRKVPLGRR EASAEQIADA
VIFLVSGSAQ YITGSIIKVD GGLSLVHA
//