Structure of PDB 4nl1 Chain B

Receptor sequence
>4nl1B (length=262) Species: 1392 (Bacillus anthracis) [Search protein sequence]
KWDYDLRCGEYTLNLNEKTLIMGILNVTPFSDGGSYNEVDAAVRHAKEMR
DEGAHIIDIGGVSVEEEIKRVVPMIQAVSKEVKLPISIDTYKAEVAKQAI
EAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDNMNYRNLMADMIA
DLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYP
VLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFVRVHDVKEMS
RMAKMMDAMIGK
3D structure
PDB4nl1 Identification and characterization of an allosteric inhibitory site on dihydropteroate synthase.
ChainB
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) V28 D54 K220 R254
Catalytic site (residue number reindexed from 1) V27 D51 K208 R242
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 Z13 B L235 M264 L223 M252 PDBbind-CN: -logKd/Ki=3.89,Kd=130uM
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:4nl1, PDBe:4nl1, PDBj:4nl1
PDBsum4nl1
PubMed24650357
UniProtQ81VW8

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