3I6B

Crystal structure of YrbI lacking the last 8 residues, in complex with Kdo and inorganic phosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
A	0009103	biological_process	lipopolysaccharide biosynthetic process
A	0016787	molecular_function	hydrolase activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
A	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
A	0046872	molecular_function	metal ion binding
B	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
B	0009103	biological_process	lipopolysaccharide biosynthetic process
B	0016787	molecular_function	hydrolase activity
B	0016788	molecular_function	hydrolase activity, acting on ester bonds
B	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
B	0046872	molecular_function	metal ion binding
C	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
C	0009103	biological_process	lipopolysaccharide biosynthetic process
C	0016787	molecular_function	hydrolase activity
C	0016788	molecular_function	hydrolase activity, acting on ester bonds
C	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
C	0046872	molecular_function	metal ion binding
D	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
D	0009103	biological_process	lipopolysaccharide biosynthetic process
D	0016787	molecular_function	hydrolase activity
D	0016788	molecular_function	hydrolase activity, acting on ester bonds
D	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
D	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19726684","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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