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1OHJ

HUMAN DIHYDROFOLATE REDUCTASE, MONOCLINIC (P21) CRYSTAL FORM

Functional Information from GO Data
ChainGOidnamespacecontents
A0000900molecular_functionmRNA regulatory element binding translation repressor activity
A0003723molecular_functionRNA binding
A0003729molecular_functionmRNA binding
A0004146molecular_functiondihydrofolate reductase activity
A0005542molecular_functionfolic acid binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006545biological_processglycine biosynthetic process
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
A0051000biological_processpositive regulation of nitric-oxide synthase activity
A0070402molecular_functionNADPH binding
A1990825molecular_functionsequence-specific mRNA binding
A2000121biological_processregulation of removal of superoxide radicals
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NDP A 187
ChainResidue
AALA9
ALYS55
ATHR56
ASER59
ALEU75
ASER76
AARG77
AGLU78
AARG91
AGLY117
ASER118
AILE16
ASER119
ATYR121
AGLU123
ACOP188
AHOH189
AGLY17
AGLY20
AASP21
ALEU22
ATRP24
AGLY53
ALYS54

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE COP A 188
ChainResidue
AILE7
AVAL8
AGLU30
APHE31
AARG32
APHE34
AGLN35
AILE60
AASN64
ALEU67
AARG70
AVAL115
ATYR121
APRO128
ANDP187

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 Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:15039552, ECO:0000269|PubMed:16222560, ECO:0000269|PubMed:19478082
ChainResidueDetails
AVAL10
AILE16
ALYS55
AARG77
AGLY117

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:2248959
ChainResidueDetails
APHE31
AARG65
AILE71

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 490
ChainResidueDetails
APRO23electrostatic stabiliser
APHE31electrostatic stabiliser

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PDB entries from 2024-04-24

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