Structure of PDB 1jqn Chain A

Receptor sequence
>1jqnA (length=874) Species: 562 (Escherichia coli) [Search protein sequence]
QYSALRSNVSMLGKVLGETIKDALGEHILERVETIRKLSKSSRAGNDANR
QELLTTLQNLSNDELLPVARAFSQFLNLANTAEQYHSISPKGEAASNPEV
IARTLRKLKNQPELSEDTIKKAVESLSLELVLTAHPTEITRRTLIHKMVE
VNACLKQLDNKDIADYEHNQLMRRLRQLIAQSWHTDEIRKLRPSPVDEAK
WGFAVVENSLWQGVPNYLRELNEQLEENLGYKLPVEFVPVRFTSWMGGDR
DGNPNVTADITRHVLLLSRWKATDLFLKDIQVLVSELSMVEATPELLALV
GEEGAAEPYRYLMKNLRSRLMATQAWLEARLKGEELPKPEGLLTQNEELW
EPLYACYQSLQACGMGIIANGDLLDTLRRVKCFGVPLVRIDIRQESTRHT
EALGELTRYLGIGDYESWSEADKQAFLIRELNSKRPLLPRNWQPSAETRE
VLDTCQVIAEAPQGSIAAYVISMAKTPSDVLAVHLLLKEAGIGFAMPVAP
LFETLDDLNNANDVMTQLLNIDWYRGLIQGKQMVMIGYSDSAKDAGVMAA
SWAQYQAQDALIKTCEKAGIELTLFHGRGGSIGRGGAPAHAALLSQPPGS
LKGGLRVTEQGEMIRFKYGLPEITVSSLSLYTGAILEANLLPPPEPKESW
RRIMDELSVISCDVYRGYVRENKDFVPYFRSATPEQELGKLPLGSRPGGV
ESLRAIPWIFAWTQNRLMLPAWLGAGTALQKVVEDGKQSELEAMCRDWPF
FSTRLGMLEMVFAKADLWLAEYYDQRLVDKALWPLGKELRNLQEEDIKVV
LAIANDSHLMADLPWIAESIQLRNIYTDPLNVLQAELLHRSRQAEKEGQE
PDPRVEQALMVTIAGIAAGMRNTG
3D structure
PDB1jqn Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases.
ChainA
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 R704
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 MN A E506 D543 E503 D540
BS02 ASP A R587 M769 K773 R832 N881 R584 M760 K764 R823 N872
BS03 DCO A R396 G540 D543 R581 R699 R393 G537 D540 R578 R696
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1jqn, PDBe:1jqn, PDBj:1jqn
PDBsum1jqn
PubMed12467579
UniProtP00864|CAPP_ECOLI Phosphoenolpyruvate carboxylase (Gene Name=ppc)

[Back to BioLiP]