Structure of PDB 2a21 Chain A

Receptor sequence
>2a21A (length=263) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
EKFLVIAGPCAIESEELLLKVGEEIKRLSEKFKEVEFVFKSSFDKANRSS
IHSFRGHGLEYGVKALRKVKEEFGLKITTDIHESWQAEPVAEVADIIQIP
AFLCRQTDLLLAAAKTGRAVNVKKGQFLAPWDTKNVVEKLKFGGAKEIYL
TERGTTFGYNNLVVDFRSLPIMKQWAKVIYDATHSVQLPGGLGDKSGGMR
EFIFPLIRAAVAVGCDGVFMETHPEPEKALSDASTQLPLSQLEGIIEAIL
EIREVASKYYETI
3D structure
PDB2a21 Electronic structure of the metal center in the Cd(2+), Zn(2+), and Cu(2+) substituted forms of KDO8P synthase: implications for catalysis.
ChainA
Resolution1.8 Å
3D
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
Enzyme Commision number 2.5.1.55: 3-deoxy-8-phosphooctulonate 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 PO4 A R1049 S1050 S1197 R48 S49 S196
BS02 ZN A C1011 H1185 E1222 D1233 C10 H184 E221 D232
BS03 PEP A K1041 K1046 Q1099 P1101 A1102 K1124 R1154 H1185 K40 K45 Q98 P100 A101 K123 R153 H184
Gene Ontology
Molecular Function
GO:0008676 3-deoxy-8-phosphooctulonate synthase activity
GO:0016740 transferase activity
Biological Process
GO:0009058 biosynthetic process
GO:0009103 lipopolysaccharide biosynthetic process
GO:0019294 keto-3-deoxy-D-manno-octulosonic acid biosynthetic process
GO:0046364 monosaccharide biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2a21, PDBe:2a21, PDBj:2a21
PDBsum2a21
PubMed19228070
UniProtO66496|KDSA_AQUAE 2-dehydro-3-deoxyphosphooctonate aldolase (Gene Name=kdsA)

[Back to BioLiP]