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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=2682653 [NCBI, ExPASy, EBI, Israel, Japan]
Edman J.C.,
Edman U.,
Cao M.,
Lundgren B.,
Kovacs J.,
Santi D.V.;
"Isolation and expression of the Pneumocystis carinii dihydrofolate reductase gene.";
Proc. Natl. Acad. Sci. U.S.A. 86:8625-8629(1989).
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[2]
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X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
DOI=10.1016/S0969-2126(94)00093-X; PubMed=7866743 [NCBI, ExPASy, EBI, Israel, Japan]
Champness J.N.,
Achari A.,
Ballantine S.P.,
Bryant P.K.,
Delves C.J.,
Stammers D.K.;
"The structure of Pneumocystis carinii dihydrofolate reductase to 1.9-A resolution.";
Structure 2:915-924(1994).
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[3]
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X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1021/bi982728m; PubMed=10194348 [NCBI, ExPASy, EBI, Israel, Japan]
Cody V.,
Galitsky N.,
Rak D.,
Luft J.R.,
Pangborn W.,
Queener S.F.;
"Ligand-induced conformational changes in the crystal structures of Pneumocystis carinii dihydrofolate reductase complexes with folate and NADP+.";
Biochemistry 38:4303-4312(1999).
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 206 AA [This is the length of the unprocessed precursor] |
Molecular weight: 23884 Da [This is the MW of the unprocessed precursor] |
CRC64: 6BA64A7019911508 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MNQQKSLTLI VALTTSYGIG RSNSLPWKLK KEISYFKRVT SFVPTFDSFE SMNVVLMGRK
70 80 90 100 110 120
TWESIPLQFR PLKGRINVVI TRNESLDLGN GIHSAKSLDH ALELLYRTYG SESSVQINRI
130 140 150 160 170 180
FVIGGAQLYK AAMDHPKLDR IMATIIYKDI HCDVFFPLKF RDKEWSSVWK KEKHSDLESW
190 200
VGTKVPHGKI NEDGFDYEFE MWTRDL
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P16184 in FASTA format |
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ExPASy Home page
CBR Canada
