Structure of PDB 2y5s Chain A

Receptor sequence
>2y5sA (length=280) Species: 95486 (Burkholderia cenocepacia) [Search protein sequence]
TFLPAPLQCGRFELTFERPLVMGILNATPARDDALRRAERMIAEGADLLD
IGGESTRPGAPPVPLDEELARVIPLVEALRPLNVPLSIDTYKPAVMRAAL
AAGADLINDIWGFRQPGAIDAVRDGNSGLCAMHMLGEPQTMQVGEPDYGD
VVTDVRDFLAARAQALRDAGVAAERICVDPGFGFGKAVVDDNYALLAALP
DTAPARPDGRAYPILAGMSRKSMLGAVIGGKPPLERVAASVAAALCAVER
GAAIVRVHDVAATVDALSVWNAVRAAARQR
3D structure
PDB2y5s Crystal Structures of Burkholderia Cenocepacia Dihydropteroate Synthase in the Apo-Form and Complexed with the Product 7,8-Dihydropteroate.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K233 R268
Catalytic site (residue number reindexed from 1) K221 R256
Enzyme Commision number 2.5.1.15: dihydropteroate synthase.
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 78H A T68 R69 D101 N120 M144 D191 F196 G229 K233 S234 R268 T56 R57 D89 N108 M132 D179 F184 G217 K221 S222 R256
Gene Ontology
Molecular Function
GO:0004156 dihydropteroate synthase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0042558 pteridine-containing compound metabolic process
GO:0044237 cellular metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046656 folic acid biosynthetic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:2y5s, PDBe:2y5s, PDBj:2y5s
PDBsum2y5s
PubMed21554707
UniProtB4E5F5

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