Structure of PDB 4nir Chain B

Receptor sequence
>4nirB (length=264) Species: 1392 (Bacillus anthracis) [Search protein sequence]
MKWDYDLRCGEYTLNLNEKTLIMGILNVTPSDGGSYNEVDAAVRHAKEMR
DEGAHIIDIGGESVSVEEEIKRVVPMIQAVSKEVKLPISIDTYKAEVAKQ
AIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDNMNYRNLADMI
ADLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGY
PVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFVRVHDVKEM
SRMAKMMDAMIGKG
3D structure
PDB4nir Identification and characterization of an allosteric inhibitory site on dihydropteroate synthase.
ChainB
Resolution1.772 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) V28 D51 K209 R243
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 6DH B E236 E260 E225 E249
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:4nir, PDBe:4nir, PDBj:4nir
PDBsum4nir
PubMed24650357
UniProtQ81VW8

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