Structure of PDB 1i2k Chain A

Receptor sequence
>1i2kA (length=269) Species: 562 (Escherichia coli) [Search protein sequence]
MFLINGHKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDAC
QRLMISCDFWPQLEQEMKTLAAEQQNGVLKVVISRGSGGRGYSTLNSGPA
TRILSVTAYPAHYDRLRNEGITLALSPVRLGRNPHLAGIKHLNRLEQVLI
RSHLEQTNADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGI
MRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMPVMPVCACGDV
SFSSATLYEYLAPLCERPN
3D structure
PDB1i2k Structure and Mechanism of Escherichia coli Aminodeoxychorismate Lyase
ChainA
Resolution1.79 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F26 T28 I139 K140 E173 V197
Catalytic site (residue number reindexed from 1) F26 T28 I139 K140 E173 V197
Enzyme Commision number 4.1.3.38: aminodeoxychorismate lyase.
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 PLP A R45 K140 E173 A176 A177 V197 G199 I200 M201 N236 A237 R45 K140 E173 A176 A177 V197 G199 I200 M201 N236 A237
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008696 4-amino-4-deoxychorismate lyase activity
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0008153 para-aminobenzoic acid biosynthetic process
GO:0046394 carboxylic acid biosynthetic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046656 folic acid biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1i2k, PDBe:1i2k, PDBj:1i2k
PDBsum1i2k
PubMed
UniProtP28305|PABC_ECOLI Aminodeoxychorismate lyase (Gene Name=pabC)

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