Structure of PDB 1gqc Chain A

Receptor sequence
>1gqcA (length=242) Species: 562 (Escherichia coli) [Search protein sequence]
SKAVIVIPARYGSSRLPGKPLLDIVGKPMIQHVYERALQVAGVAEVWVAT
DDPRVEQAVQAFGGKAIMTRNDHESGTDRLVEVMHKVEADIYINLQGDEP
MIRPRDVETLLQGMRDDPALPVATLCHAISAAEAAEPSTVKVVVNTRQDA
LYFSRSPIPYPRNAEKARYLKHVGIYAYRRDVLQNYSQLPESMPEQAESL
EQLRLMNAGINIRTFEVAATGPGVDTPACLEKVRALMAQELA
3D structure
PDB1gqc Catalytic Mechanism of Cmp:2-Keto-3-Deoxy-Manno-Octonic Acid Synthetase as Derived from Complexes with Reaction Educt and Product.
ChainA
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.7.38: 3-deoxy-manno-octulosonate cytidylyltransferase.
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 MG A Q96 D98 Q96 D98
BS02 CMK A R10 H73 E74 S75 G76 R79 Q96 V140 R155 H172 G174 Y176 L200 E201 Q202 R10 H73 E74 S75 G76 R79 Q96 V140 R155 H172 G174 Y176 L200 E201 Q202
Gene Ontology
Molecular Function
GO:0008690 3-deoxy-manno-octulosonate cytidylyltransferase activity
GO:0016779 nucleotidyltransferase activity
Biological Process
GO:0009103 lipopolysaccharide biosynthetic process
GO:0033468 CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:1gqc, PDBe:1gqc, PDBj:1gqc
PDBsum1gqc
PubMed11802716
UniProtP42216|KPSU5_ECOLX 3-deoxy-manno-octulosonate cytidylyltransferase (Gene Name=kpsU)

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