Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1MVT

Analysis of Two Polymorphic Forms of a Pyrido[2,3-d]pyrimidine N9-C10 Reverse-Bridge Antifolate Binary Complex with Human Dihydrofolate Reductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000900molecular_functionmRNA regulatory element binding translation repressor activity
A0003723molecular_functionRNA binding
A0003729molecular_functionmRNA binding
A0004146molecular_functiondihydrofolate reductase activity
A0005515molecular_functionprotein binding
A0005542molecular_functionfolic acid binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006729biological_processtetrahydrobiopterin biosynthetic process
A0006730biological_processone-carbon metabolic process
A0008144molecular_functionobsolete drug binding
A0016491molecular_functionoxidoreductase activity
A0017148biological_processnegative regulation of translation
A0031103biological_processaxon regeneration
A0031427biological_processresponse to methotrexate
A0046452biological_processdihydrofolate metabolic process
A0046653biological_processtetrahydrofolate metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046655biological_processfolic acid metabolic process
A0050661molecular_functionNADP binding
A0070402molecular_functionNADPH binding
A1990825molecular_functionsequence-specific mRNA binding
A2000121biological_processregulation of removal of superoxide radicals
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 188
ChainResidue
AGLY53
ALYS54
ALYS55
ATHR56
AGLY117
AVAL120
AHOH201
AHOH207

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 189
ChainResidue
AARG77
AGLU78
AHOH207
ASER76

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE DTM A 187
ChainResidue
AILE7
AVAL8
AALA9
AASP21
ALEU22
AGLU30
APHE31
APHE34
APRO61
AASN64
AVAL115
ATYR121
ATHR136
AHOH195

Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues24
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGkngdLPWpplrnEfryFqrmT
ChainResidueDetails
AGLY15-THR38

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues181
DetailsDomain: {"description":"DHFR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00660","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15039552","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16222560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19478082","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"2248959","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dhf
ChainResidueDetails
ALEU22
AGLU30

site_idMCSA1
Number of Residues2
DetailsM-CSA 490
ChainResidueDetails
ALEU22electrostatic stabiliser
AGLU30electrostatic stabiliser

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon