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 | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| B | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| C | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| C | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| C | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| C | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| D | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| D | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| D | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| D | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| E | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| E | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| E | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| E | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| F | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| F | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| F | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| F | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| G | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| G | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| G | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| G | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| H | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| H | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| H | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| H | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| I | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| I | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| I | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| I | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| J | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| J | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| J | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| J | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| K | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| K | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| K | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| K | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| L | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| L | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| L | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| L | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| M | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| M | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| M | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| M | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| N | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| N | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| N | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| N | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| O | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| O | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| O | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| O | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
| P | 0008781 | molecular_function | N-acylneuraminate cytidylyltransferase activity |
| P | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| P | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| P | 0019143 | molecular_function | 3-deoxy-manno-octulosonate-8-phosphatase activity |
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 |
