Structure of PDB 2bmb Chain A

Receptor sequence
>2bmbA (length=513) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
SWKRAFLAFGSNIGDRFKHIQMALQLLSREKTVKLRNISSIFESEPMYFK
DQTPFMNGCVEVETLLTPSELLKLCKKIEYEELQRTIDLDIVMFLNSAGE
DIIVNEPDLNIPHPRMLERTFVLEPLCELISPVHLHPVTAEPIVDHLKQL
YDKQHDEDTLWKLVPLPYRSGVEPRFLKFKTATKTNRITVSPTYIMAIFN
ATPDSFSDGGEHFADIESQLNDIIKLCKDALYLHESVIIDVGGCSTRPNS
IQASEEEEIRRSIPLIKAIRESTELPQDKVILSIDTYRSNVAKEAIKVGV
DIINDISGGLFDSNMFAVIAENPEICYILSHTRGDISTMNRLAHYENFAL
GDSIQQEFVHNTDIQQLDDLKDKTVLIRNVGQEIGERYIKAIDNGVKRWQ
ILIDPGLGFAKTWKQNLQIIRHIPILKNYSFTMNSNNSQVYVNLRNMPVL
LGPSRKKFIGHITKDVDAKQRDFATGAVVASCIGFGSDMVRVHDVKNCSK
SIKLADAIYKGLE
3D structure
PDB2bmb The Three-Dimensional Structure of the Bifunctional 6-Hydroxymethyl-7,8-Dihydropterin Pyrophosphokinase/Dihydropteroate Synthase of Saccharomyces Cerevisiae
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R420 D432 D434 K807 R842
Catalytic site (residue number reindexed from 1) R85 D88 D90 K456 R491
Enzyme Commision number 2.5.1.15: dihydropteroate synthase.
2.7.6.3: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase.
4.1.2.25: dihydroneopterin aldolase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PMM A R598 N655 I657 D755 F760 G803 K807 R842 H844 R247 N304 I306 D404 F409 G452 K456 R491 H493
BS02 PMM A S379 E380 M382 Y383 F390 N392 R463 F465 S44 E45 M47 Y48 F55 N57 R119 F121
Gene Ontology
Molecular Function
GO:0003848 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
GO:0004156 dihydropteroate synthase activity
Biological Process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0042558 pteridine-containing compound metabolic process
GO:0044237 cellular metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2bmb, PDBe:2bmb, PDBj:2bmb
PDBsum2bmb
PubMed15826662
UniProtP53848|FOL1_YEAST Folic acid synthesis protein FOL1 (Gene Name=FOL1)

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