Structure of PDB 3tyc Chain A

Receptor sequence
>3tycA (length=266) Species: 191218 (Bacillus anthracis str. A2012) [Search protein sequence]
KWDYDLRCGEYTLNLNEKTLIMGILNVTPDSFSDGGSYNEVDAAVRHAKE
MRDEGAHIIDIGGEVSVEEEIKRVVPMIQAVSKEVKLPISIDTYKAEVAK
QAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDNMNYRNLMAD
MIADLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVL
GYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFVRVHDVK
EMSRMAKMMDAMIGKG
3D structure
PDB3tyc Catalysis and sulfa drug resistance in dihydropteroate synthase.
ChainA
Resolution2.303 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V28 D54 K220 R254
Catalytic site (residue number reindexed from 1) V27 D53 K211 R245
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 XHP A D101 N120 I122 M145 D184 F189 G216 K220 R254 D92 N111 I113 M136 D175 F180 G207 K211 R245
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:3tyc, PDBe:3tyc, PDBj:3tyc
PDBsum3tyc
PubMed22383850
UniProtQ81VW8

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