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3Q1H

Crystal Structure of Dihydrofolate Reductase from Yersinia pestis

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 Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 170
ChainResidue
AGLY44
AARG45
ALYS46
ATHR47
AGLY97
AARG99
AVAL100
AHOH163
AHOH301

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 171
ChainResidue
AARG45
ASER64
ASER65
AARG99

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

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PDB entries from 2024-11-06

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