Structure of PDB 1fiy Chain A

Receptor sequence
>1fiyA (length=873) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
QYSALRSNVSMLGKVLGETIKDALGEHILERVETIRKLSKSSRAGNDANR
QELLTTLQNLSNDELLPVARAFSQFLNLANTAEQYHSISPKGEAASNPEV
IARTLRKLKNQPELSEDTIKKAVESLSLELVLTAHPTEITRRTLIHKMVE
VNACLKQLDNKDIADYEHNQLMRRLRQLIAQSWHTDEIRKLRPSPVDEAK
WGFAVVENSLWQGVPNYLRELNEQLEENLGYKLPVEFVPVRFTSWMGGDR
DGNPNVTADITRHVLLLSRWKATDLFLKDIQVLVSELSMVEATPELLALV
GEEGAAEPYRYLMKNLRSRLMATQAWLEARLKGEELPKPEGLLTQNEELW
EPLYACYQSLQACGMGIIANGDLLDTLRRVKCFGVPLVRIDIRQESTRHT
EALGELTRYLGIGDYESWSEADKQAFLIRELNSKRPLLPRNWQPSAETRE
VLDTCQVIAEAPQGSIAAYVISMAKTPSDVLAVHLLLKEAGIGFAMPVAP
LFETLDDLNNANDVMTQLLNIDWYRGLIQGKQMVMIGYSDSAKDAGVMAA
SWAQYQAQDALIKTCEKAGIELTLFHGRGGSIGRGGAPAHAALLSQPPGS
LKGGLRVTEQGEMIRFKYGLPEITVSSLSLYTGAILEANLLPPPEPKESW
RRIMDELSVISCDVYRGYVRENKDFVPYFRSATPEQELGKLPLGSRPAVE
SLRAIPWIFAWTQNRLMLPAWLGAGTALQKVVEDGKQSELEAMCRDWPFF
STRLGMLEMVFAKADLWLAEYYDQRLVDKALWPLGKELRNLQEEDIKVVL
AIANDSHLMADLPWIAESIQLRNIYTDPLNVLQAELLHRSRQAEKEGQEP
DPRVEQALMVTIAGIAAGMRNTG
3D structure
PDB1fiy Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H138 R396 E506 D543 R581 R713
Catalytic site (residue number reindexed from 1) H135 R393 E503 D540 R578 R703
Enzyme Commision number 4.1.1.31: phosphoenolpyruvate carboxylase.
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 ASP A R587 M769 K773 I825 R832 R880 N881 R584 M759 K763 I815 R822 R870 N871
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0008964 phosphoenolpyruvate carboxylase activity
GO:0016829 lyase activity
GO:0042802 identical protein binding
Biological Process
GO:0006094 gluconeogenesis
GO:0006099 tricarboxylic acid cycle
GO:0006107 oxaloacetate metabolic process
GO:0015977 carbon fixation
GO:0051289 protein homotetramerization
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:1fiy, PDBe:1fiy, PDBj:1fiy
PDBsum1fiy
PubMed9927652
UniProtP00864|CAPP_ECOLI Phosphoenolpyruvate carboxylase (Gene Name=ppc)

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