Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5FDA

The high resolution structure of apo form dihydrofolate reductase from Yersinia pestis at 1.55 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0016491molecular_functionoxidoreductase activity
A0046452biological_processdihydrofolate metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046655biological_processfolic acid metabolic process
A0046872molecular_functionmetal ion binding
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CL A 201
ChainResidue
AASN35
AASN35
ALYS39
ALYS39

site_idAC2
Number of Residues6
Detailsbinding site for residue CL A 202
ChainResidue
AHOH417
AASN38
AASN38
ALYS39
ALYS39
AHOH417

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 203
ChainResidue
ASER149
ASER149

Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGmenaMPWhlpa.DlawFkrnT
ChainResidueDetails
AVAL14-THR36

222036

PDB entries from 2024-07-03

PDB statisticsPDBj update infoContact PDBjnumon