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1LUD

SOLUTION STRUCTURE OF DIHYDROFOLATE REDUCTASE COMPLEXED WITH TRIMETHOPRIM AND NADPH, 24 STRUCTURES

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0016491molecular_functionoxidoreductase activity
A0031427biological_processresponse to methotrexate
A0046452biological_processdihydrofolate metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046655biological_processfolic acid metabolic process
A0046677biological_processresponse to antibiotic
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NDP A 168
ChainResidue
ATRP5
ATHR45
ALEU62
ATHR63
AHIS64
AGLN65
AALA97
AGLY99
AALA100
AGLN101
AILE102
AALA6
ATRR170
AILE13
AGLY14
ALYS15
AGLY17
AGLY42
AARG43
AARG44

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TRR A 170
ChainResidue
ALEU4
ATRP5
AALA6
AGLY17
ALEU19
AASP26
ALEU27
APHE30
APHE49
APRO50
AALA97
ATHR116
ANDP168

Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. LIGkdghLPWhlpd.DlhyFraqT
ChainResidueDetails
ALEU12-THR34

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:6815179
ChainResidueDetails
ATRP5
ALEU27
AALA32
ATHR58
AARG117

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:6815179
ChainResidueDetails
AALA6
AGLY14
AARG43
ATHR63
AALA80
AGLY98

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: May be important for enzyme function
ChainResidueDetails
AHIS22

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dhf
ChainResidueDetails
ALEU19
AASP26

site_idMCSA1
Number of Residues9
DetailsM-CSA 112
ChainResidueDetails
ATRP5steric role
APRO20enhance reactivity
AHIS22activator, hydrogen bond donor
ALEU27hydrogen bond acceptor, modifies pKa
AHIS28steric locator
AARG31steric locator
APRO55steric locator
AVAL95steric role
AARG117electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-06-26

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