Structure of PDB 1l5j Chain A

Receptor sequence
>1l5jA (length=862) Species: 562 (Escherichia coli) [Search protein sequence]
MLEEYRKHVAERAAEGIAPKPLDANQMAALVELLKNPPAGEEEFLLDLLT
NRVPPGVDEAAYVKAGFLAAIAKGEAKSPLLTPEKAIELLGTMQGGYNIH
PLIDALDDAKLAPIAAKALSHTLLMFDNFYDVEEKAKAGNEYAKQVMQSW
ADAEWFLNRPALAEKLTVTVFKVTGETNTDDLSPAPDAWSRPDIPLHALA
MLKNAREGIEPDQPGVVGPIKQIEALQQKGFPLAYVGDVVGTGSSRKSAT
NSVLWFMGDDIPHVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSN
LNMGDVIDVYPYKGEVRNHETGELLATFELKTDVLIDEVRAGGRIPLIIG
RGLTTKAREALGLPHSDVFRQAKDVAESDRGFSLAQKMVGRACGVKGIRP
GAYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPK
PVDVNTHHTLPDFIMNRGGVSLRPGDGVIHSWLNRMLLPDTVGTGGDSHT
RFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLV
HAIPLYAIKQGLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASA
ERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDRRTLERRIQGMEK
WLANPELLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARPLSAVQGE
KIDEVFIGSCMTNIGHFRAAGKLLDAHKGQLPTRLWVAPPTRMDAAQLTE
EGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLGTG
ANVFLASAELAAVAALIGKLPTPEEYQTYVAQVDKTAVDTYRYLNFNQLS
QYTEKADGVIFQ
3D structure
PDB1l5j E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D497
Catalytic site (residue number reindexed from 1) D497
Enzyme Commision number 4.2.1.3: aconitate hydratase.
4.2.1.99: 2-methylisocitrate dehydratase.
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 F3S A H444 V478 H499 S709 C710 C769 C772 T790 H444 V478 H499 S709 C710 C769 C772 T790
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0003729 mRNA binding
GO:0003730 mRNA 3'-UTR binding
GO:0003994 aconitate hydratase activity
GO:0005515 protein binding
GO:0016829 lyase activity
GO:0046872 metal ion binding
GO:0047456 2-methylisocitrate dehydratase activity
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006097 glyoxylate cycle
GO:0006099 tricarboxylic acid cycle
GO:0006417 regulation of translation
GO:0019629 propionate catabolic process, 2-methylcitrate cycle
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:1l5j, PDBe:1l5j, PDBj:1l5j
PDBsum1l5j
PubMed11992126
UniProtP36683|ACNB_ECOLI Aconitate hydratase B (Gene Name=acnB)

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