Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2R8Y

Crystal structure of YrbI phosphatase from Escherichia coli in a complex with Ca

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
I	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
I	0009103	biological_process	lipopolysaccharide biosynthetic process
I	0016787	molecular_function	hydrolase activity
I	0016788	molecular_function	hydrolase activity, acting on ester bonds
I	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
I	0046872	molecular_function	metal ion binding
J	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
J	0009103	biological_process	lipopolysaccharide biosynthetic process
J	0016787	molecular_function	hydrolase activity
J	0016788	molecular_function	hydrolase activity, acting on ester bonds
J	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
J	0046872	molecular_function	metal ion binding
K	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
K	0009103	biological_process	lipopolysaccharide biosynthetic process
K	0016787	molecular_function	hydrolase activity
K	0016788	molecular_function	hydrolase activity, acting on ester bonds
K	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
K	0046872	molecular_function	metal ion binding
L	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
L	0009103	biological_process	lipopolysaccharide biosynthetic process
L	0016787	molecular_function	hydrolase activity
L	0016788	molecular_function	hydrolase activity, acting on ester bonds
L	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
L	0046872	molecular_function	metal ion binding
M	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
M	0009103	biological_process	lipopolysaccharide biosynthetic process
M	0016787	molecular_function	hydrolase activity
M	0016788	molecular_function	hydrolase activity, acting on ester bonds
M	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
M	0046872	molecular_function	metal ion binding
N	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
N	0009103	biological_process	lipopolysaccharide biosynthetic process
N	0016787	molecular_function	hydrolase activity
N	0016788	molecular_function	hydrolase activity, acting on ester bonds
N	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
N	0046872	molecular_function	metal ion binding
O	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
O	0009103	biological_process	lipopolysaccharide biosynthetic process
O	0016787	molecular_function	hydrolase activity
O	0016788	molecular_function	hydrolase activity, acting on ester bonds
O	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
O	0046872	molecular_function	metal ion binding
P	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
P	0009103	biological_process	lipopolysaccharide biosynthetic process
P	0016787	molecular_function	hydrolase activity
P	0016788	molecular_function	hydrolase activity, acting on ester bonds
P	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
P	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

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

Chain	Residue
A	ASP32
A	ASP34
A	ASP125
A	HOH311
B	HOH359
B	HOH383

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

Chain	Residue
B	HOH332
C	HOH305
C	HOH340
B	ASP32
B	ASP34
B	ASP125

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 203

Chain	Residue
C	ASP32
C	ASP34
C	ASP125
C	HOH348
D	HOH347

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 204

Chain	Residue
D	ASP32
D	ASP34
D	ASP125
D	HOH334
D	HOH373

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA E 205

Chain	Residue
E	ASP32
E	ASP34
E	ASP125
E	HOH334

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

Chain	Residue
F	ASP32
F	ASP34
F	ASP125
F	HOH325
F	HOH344
G	HOH388

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

Chain	Residue
G	ASP32
G	ASP34
G	ASP125
G	HOH330
H	HOH309
H	HOH337

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

Chain	Residue
E	HOH329
E	HOH372
H	ASP32
H	ASP34
H	ASP125
H	HOH317

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA I 209

Chain	Residue
I	ASP32
I	ASP34
I	ASP125
I	HOH861

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA J 210

Chain	Residue
J	ASP32
J	ASP34
J	ASP125
J	HOH417

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA K 211

Chain	Residue
K	ASP32
K	ASP34
K	ASP125

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA L 212

Chain	Residue
L	ASP32
L	ASP34
L	ASP125

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA M 213

Chain	Residue
M	ASP32
M	ASP34
M	ASP125
M	HOH829

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA N 214

Chain	Residue
N	ASP32
N	ASP34
N	ASP125
N	HOH331

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA O 215

Chain	Residue
O	ASP32
O	ASP34
O	ASP125
O	HOH335

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA P 216

Chain	Residue
P	ASP32
P	ASP34
P	ASP125
P	HOH938

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 301

Chain	Residue
A	ASP32
A	GLY77
A	LYS102
B	HOH359
B	HOH361

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 302

Chain	Residue
B	ASP32
B	GLY77
B	LYS102
C	HOH340

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL C 303

Chain	Residue
C	ASP32
C	GLY77
C	LYS102
D	HOH347

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL D 304

Chain	Residue
D	ASP32
D	GLY77
D	LYS102
D	HOH373

site_id	CC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL E 305

Chain	Residue
E	LYS102

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL F 306

Chain	Residue
F	ASP32
F	GLY77
F	LYS102
G	HOH388

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL G 307

Chain	Residue
H	HOH337
G	ASP32
G	GLY77
G	LYS102

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL H 308

Chain	Residue
E	HOH329
H	ASP32
H	GLY77
H	LYS102

site_id	CC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL I 309

Chain	Residue
I	ASP32
I	GLY77
I	LYS102

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL J 310

Chain	Residue
J	ASP32
J	GLY77
J	LYS102

site_id	CC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL K 311

Chain	Residue
K	ASP32
K	GLY77
K	LYS102

site_id	DC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL L 312

Chain	Residue
L	GLY77
L	LYS102

site_id	DC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL M 313

Chain	Residue
M	ASP32
M	GLY77
M	LYS102

site_id	DC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL N 314

Chain	Residue
N	ASP32
N	GLY77
N	LYS102

site_id	DC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL O 315

Chain	Residue
O	ASP32
O	GLY77
O	LYS102

site_id	DC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL P 316

Chain	Residue
P	ASP32
P	GLY77
P	LYS102

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	176
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)