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3K2H

Co-crystal structure of dihydrofolate reductase/thymidylate synthase from Babesia bovis with dUMP, Pemetrexed and NADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004146molecular_functiondihydrofolate reductase activity
A0004799molecular_functionthymidylate synthase activity
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
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
B0000166molecular_functionnucleotide binding
B0004146molecular_functiondihydrofolate reductase activity
B0004799molecular_functionthymidylate synthase activity
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006231biological_processdTMP biosynthetic process
B0006730biological_processone-carbon metabolic process
B0008168molecular_functionmethyltransferase activity
B0009165biological_processnucleotide biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016741molecular_functiontransferase activity, transferring one-carbon groups
B0032259biological_processmethylation
B0046654biological_processtetrahydrofolate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE UMP A 512
ChainResidue
AARG248
AASN424
AHIS454
ATYR456
ALYA513
AHOH566
AHOH730
BARG373
BARG374
ALEU390
ACYS393
AHIS394
AGLN412
AARG413
ASER414
ACYS415
AASP416

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE LYA A 513
ChainResidue
AALA278
ASER281
AILE306
AASN310
ALEU390
AASP416
ALEU419
AGLY420
APHE423
ATYR456
AMET509
ASER510
AUMP512
AHOH559
AHOH653
AHOH690
AHOH694
AHOH710
AHOH735
AHOH794
AHOH843

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE LYA A 514
ChainResidue
APHE14
AVAL15
AALA16
AASP37
APHE38
AARG39
ALEU41
AARG42
ASER77
AARG83
ALEU123
ATYR129
ATHR144
ANAP515
AHOH571
AHOH575
AHOH608
AHOH664

site_idAC4
Number of Residues32
DetailsBINDING SITE FOR RESIDUE NAP A 515
ChainResidue
AVAL15
AALA16
AILE23
AGLY24
AHIS25
AASN27
AGLN28
AILE29
ATRP31
AGLY66
AARG67
ALYS68
ATHR69
ASER72
ALEU88
ASER89
AARG90
ATHR91
AGLU102
AASP103
ALEU104
ALEU123
AGLY125
ASER126
APHE127
ATYR129
AGLU131
ATHR154
ALYA514
AHOH587
AHOH721
BARG305

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 516
ChainResidue
AGLN358
AGLU361
AILE376
AHOH858
BTRP380
BVAL382
BLEU385

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 517
ChainResidue
BGLN358
BGLU361
BILE362
BILE376
BHOH622
ATRP380
AVAL382
ALEU385
BILE356

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 517
ChainResidue
AARG374
BASN319
BALA389
BPRO391
BHOH691

site_idAC8
Number of Residues17
DetailsBINDING SITE FOR RESIDUE UMP B 512
ChainResidue
AARG373
AARG374
BARG248
BLEU390
BCYS393
BHIS394
BGLN412
BARG413
BSER414
BCYS415
BASP416
BASN424
BHIS454
BTYR456
BLYA513
BHOH544
BHOH717

site_idAC9
Number of Residues22
DetailsBINDING SITE FOR RESIDUE LYA B 513
ChainResidue
BALA278
BSER281
BILE306
BASN310
BLEU390
BASP416
BLEU419
BGLY420
BPHE423
BMET509
BSER510
BUMP512
BHOH524
BHOH545
BHOH552
BHOH556
BHOH566
BHOH595
BHOH718
BHOH737
BHOH763
BHOH804

site_idBC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE LYA B 514
ChainResidue
BPHE14
BVAL15
BALA16
BASP37
BPHE38
BARG39
BLEU41
BARG42
BLEU80
BARG83
BLEU123
BTHR144
BNAP515
BHOH534
BHOH629
BHOH713

site_idBC2
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAP B 515
ChainResidue
AARG305
BVAL15
BALA16
BILE23
BGLY24
BASN27
BGLN28
BILE29
BTRP31
BGLY66
BARG67
BLYS68
BTHR69
BSER72
BLEU88
BSER89
BARG90
BTHR91
BGLU102
BASP103
BLEU123
BGLY125
BSER126
BPHE127
BTYR129
BGLU131
BTHR154
BLYA514

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 516
ChainResidue
AARG248
AALA389
APRO391
AHOH820
BARG374

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 518
ChainResidue
APHE340
AGLY341
AASN381
ASER383
BPHE340
BGLY341
BASN381
BSER383

Functional Information from PROSITE/UniProt
site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrlIvcsWNvsdlkkma.....LpPCHcffQFyV
ChainResidueDetails
AARG373-VAL401

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PDB entries from 2024-06-12

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