Structure of PDB 1gqc Chain B

Receptor sequence
>1gqcB (length=241) Species: 562 (Escherichia coli) [Search protein sequence]
SKAVIVIPARYGSSRLPGKPLLDIVGKPMIQHVYERALQVAGVAEVWVAT
DDPRVEQAVQAFGGKAIMTRNDHESGTDRLVEVMHKVEADIYINLQGDEP
MIRPRDVETLLQGMRDDPALPVATLCHAISAAEAAEPSTVKVVVNTRQDA
LYFSRSPIPYPRNAEKARYLKHVGIYAYRRDVLQNYSQLPESMPEQAESL
EQLRLMNAGINIRTFEVAATGPGVDTPACLEKVRALMAQEL
3D structure
PDB1gqc Catalytic Mechanism of Cmp:2-Keto-3-Deoxy-Manno-Octonic Acid Synthetase as Derived from Complexes with Reaction Educt and Product.
ChainB
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 B D98 D225 D98 D225
BS02 C5P B P8 A9 R10 E74 S75 G76 R79 Q96 G97 P8 A9 R10 E74 S75 G76 R79 Q96 G97
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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Molecular Function

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Biological Process

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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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