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3CL9

Structure of bifunctional TcDHFR-TS in complex with MTX

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0004799molecular_functionthymidylate synthase activity
A0006231biological_processdTMP biosynthetic process
A0006730biological_processone-carbon metabolic process
A0008168molecular_functionmethyltransferase activity
A0009165biological_processnucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016741molecular_functiontransferase activity, transferring one-carbon groups
A0032259biological_processmethylation
A0046654biological_processtetrahydrofolate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 801
ChainResidue
AARG233
AARG235

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 802
ChainResidue
AARG177
ATRP206
AARG208
ALEU230
AARG249
AGLU250

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAP A 601
ChainResidue
AILE35
ASER40
ATRP43
AGLY77
AARG78
ALYS79
ATHR80
ASER83
ALEU99
ASER100
ASER101
ATHR102
AASN129
AGLY130
AGLY131
AILE154
AGLY155
AGLY156
AGLY157
ASER158
ATYR160
AALA28

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MTX A 602
ChainResidue
AALA28
AASP48
AMET49
APHE52
AARG53
ATHR80
ASER83
APHE88
ALEU91
AARG94
AILE154
ATYR160
ATHR178

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE UMP A 603
ChainResidue
AARG257
AARG383
AARG384
ACYS403
AHIS404
AGLN422
AARG423
ASER424
AASP426
AGLY430
AASN434
AHIS464
ATYR466

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 701
ChainResidue
APHE51
APHE227

Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGdgrsIPWnvpe.DmkfFrdvT
ChainResidueDetails
AGLY34-THR56

site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrmLftaWNpsalprma.....LpPCHllaQFyV
ChainResidueDetails
AARG383-VAL411

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ACYS403

site_idSWS_FT_FI2
Number of Residues15
DetailsBINDING:
ChainResidueDetails
AVAL26
ATHR178
AARG257
AHIS404
AGLN422
AASN434
AHIS464
AALA28
AGLY34
AASP48
AARG78
ALEU99
AILE154
AGLY155
ATYR160

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b02
ChainResidueDetails
ACYS403
AASN434
ASER437

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b02
ChainResidueDetails
AASP48
AILE41

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1b02
ChainResidueDetails
AASP426
AASP462
ACYS403
AHIS464
ASER424
AGLU295

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PDB entries from 2024-07-24

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