Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2R8E

Crystal structure of YrbI from Escherichia coli in complex with Mg

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
E	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
E	0009103	biological_process	lipopolysaccharide biosynthetic process
E	0016787	molecular_function	hydrolase activity
E	0016788	molecular_function	hydrolase activity, acting on ester bonds
E	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
E	0046872	molecular_function	metal ion binding
F	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
F	0009103	biological_process	lipopolysaccharide biosynthetic process
F	0016787	molecular_function	hydrolase activity
F	0016788	molecular_function	hydrolase activity, acting on ester bonds
F	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
F	0046872	molecular_function	metal ion binding
G	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
G	0009103	biological_process	lipopolysaccharide biosynthetic process
G	0016787	molecular_function	hydrolase activity
G	0016788	molecular_function	hydrolase activity, acting on ester bonds
G	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
G	0046872	molecular_function	metal ion binding
H	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
H	0009103	biological_process	lipopolysaccharide biosynthetic process
H	0016787	molecular_function	hydrolase activity
H	0016788	molecular_function	hydrolase activity, acting on ester bonds
H	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 201

Chain	Residue
A	ASP32
A	ASP34
A	ASP125
A	HOH345
A	HOH346
A	HOH347

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 202

Chain	Residue
B	HOH351
B	HOH352
B	HOH353
B	ASP32
B	ASP34
B	ASP125

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 203

Chain	Residue
C	ASP32
C	ASP34
C	ASP125
C	HOH355
C	HOH356
C	HOH474

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 204

Chain	Residue
D	ASP32
D	ASP34
D	ASP125
D	HOH366
D	HOH367
D	HOH368

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 205

Chain	Residue
E	ASP32
E	ASP34
E	ASP125
E	HOH472
E	HOH473
G	HOH478

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG F 206

Chain	Residue
F	ASP32
F	ASP34
F	ASP125
F	HOH478
H	HOH488
H	HOH489

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG G 207

Chain	Residue
F	HOH479
G	ASP32
G	ASP34
G	ASP125
G	HOH479
G	HOH480

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG H 208

Chain	Residue
E	HOH474
H	ASP32
H	ASP34
H	ASP125
H	HOH490
H	HOH491

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL F 305

Chain	Residue
F	ASP32
F	GLY77
F	LYS102
H	HOH489

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL E 306

Chain	Residue
E	ASP32
E	GLY77
E	LYS102
G	HOH478

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL G 307

Chain	Residue
F	HOH479
G	ASP32
G	GLY77
G	LYS102

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL H 308

Chain	Residue
E	HOH474
H	ASP32
H	GLY77
H	LYS102

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	88
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19726684","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)