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6KCL

Crystal structure of Plasmodium falciparum HPPK-DHPS A437G/K540E with pterin and p-hydroxybenzoate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003848molecular_function2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
A0004156molecular_functiondihydropteroate synthase activity
A0005524molecular_functionATP binding
A0005740cellular_componentmitochondrial envelope
A0005829cellular_componentcytosol
A0009396biological_processfolic acid-containing compound biosynthetic process
A0016301molecular_functionkinase activity
A0042558biological_processpteridine-containing compound metabolic process
A0044237biological_processcellular metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046656biological_processfolic acid biosynthetic process
A0046872molecular_functionmetal ion binding
B0003848molecular_function2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
B0004156molecular_functiondihydropteroate synthase activity
B0005524molecular_functionATP binding
B0005740cellular_componentmitochondrial envelope
B0005829cellular_componentcytosol
B0009396biological_processfolic acid-containing compound biosynthetic process
B0016301molecular_functionkinase activity
B0042558biological_processpteridine-containing compound metabolic process
B0044237biological_processcellular metabolic process
B0046654biological_processtetrahydrofolate biosynthetic process
B0046656biological_processfolic acid biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue PE0 A 801
ChainResidue
AASP482
AARG686
APHB802
AGOL804
AHOH912
AASN502
AILE504
AMET529
AASP575
APHE580
APHE603
AGLY605
ALYS609

site_idAC2
Number of Residues6
Detailsbinding site for residue PHB A 802
ChainResidue
AGLY579
APHE580
ALYS609
AARG610
APE0801
AHOH940

site_idAC3
Number of Residues16
Detailsbinding site for residue ATP A 803
ChainResidue
ALEU181
ALYS185
AASP208
AASP210
AILE211
AASN312
AILE313
AGLU314
APHE315
ALEU316
ASER317
AHIS320
AARG326
AMG805
AHOH903
AHOH961

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 804
ChainResidue
AASN396
AARG686
AHIS688
APE0801
AHOH957

site_idAC5
Number of Residues4
Detailsbinding site for residue MG A 805
ChainResidue
AASP208
AASP210
AATP803
AHOH961

site_idAC6
Number of Residues5
Detailsbinding site for residue CA A 806
ChainResidue
AGLU42
AGLY46
AGLU99
AHOH955
AHOH998

site_idAC7
Number of Residues5
Detailsbinding site for residue ACT A 807
ChainResidue
AHIS530
AARG532
AASP550
ATYR554
AHOH982

site_idAC8
Number of Residues13
Detailsbinding site for residue PE0 B 801
ChainResidue
BASP482
BASN502
BILE504
BMET529
BASP575
BPHE580
BPHE603
BGLY605
BLYS609
BARG686
BPHB802
BGOL804
BHOH942

site_idAC9
Number of Residues7
Detailsbinding site for residue PHB B 802
ChainResidue
BGLY579
BPHE580
BLYS609
BARG610
BPE0801
BGOL804
BHOH935

site_idAD1
Number of Residues16
Detailsbinding site for residue ATP B 803
ChainResidue
BLEU181
BLYS185
BASP208
BASP210
BILE211
BASN312
BILE313
BGLU314
BPHE315
BLEU316
BSER317
BILE318
BARG326
BMG805
BHOH940
BHOH966

site_idAD2
Number of Residues5
Detailsbinding site for residue GOL B 804
ChainResidue
BARG686
BHIS688
BPE0801
BPHB802
BHOH925

site_idAD3
Number of Residues4
Detailsbinding site for residue MG B 805
ChainResidue
BASP208
BASP210
BATP803
BHOH966

site_idAD4
Number of Residues3
Detailsbinding site for residue CA B 806
ChainResidue
BGLU42
BGLY46
BGLU99

site_idAD5
Number of Residues7
Detailsbinding site for residue ACT B 807
ChainResidue
AASN487
AASN510
BHIS530
BARG532
BTYR554
BHOH937
BHOH950

Functional Information from PROSITE/UniProt
site_idPS00793
Number of Residues14
DetailsDHPS_2 Dihydropteroate synthase signature 2. GAsVIDIGGesSgP
ChainResidueDetails
AGLY425-PRO438

219869

PDB entries from 2024-05-15

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