2R8Z
Crystal structure of YrbI phosphatase from Escherichia coli in complex with a phosphate and a calcium ion
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 | PO4202 |
| A | HOH203 |
| A | HOH204 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 202 |
| Chain | Residue |
| B | ASP125 |
| B | PO4203 |
| B | HOH205 |
| A | HOH302 |
| B | ASP32 |
| B | ASP34 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 203 |
| Chain | Residue |
| C | ASP32 |
| C | ASP34 |
| C | ASP125 |
| C | PO4204 |
| C | HOH205 |
| C | HOH206 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 204 |
| Chain | Residue |
| C | HOH207 |
| D | ASP32 |
| D | ASP34 |
| D | ASP125 |
| D | PO4205 |
| D | HOH209 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA E 205 |
| Chain | Residue |
| E | ASP32 |
| E | ASP34 |
| E | ASP125 |
| E | PO4206 |
| E | HOH208 |
| H | HOH210 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA F 206 |
| Chain | Residue |
| F | ASP32 |
| F | ASP34 |
| F | ASP125 |
| F | PO4207 |
| F | HOH238 |
| F | HOH252 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA G 207 |
| Chain | Residue |
| G | ASP32 |
| G | ASP34 |
| G | ASP125 |
| G | PO4208 |
| G | HOH210 |
| G | HOH400 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA H 208 |
| Chain | Residue |
| G | HOH212 |
| H | ASP32 |
| H | ASP34 |
| H | ASP125 |
| H | PO4209 |
| H | HOH211 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA I 209 |
| Chain | Residue |
| I | ASP32 |
| I | ASP34 |
| I | ASP125 |
| I | PO4210 |
| I | HOH211 |
| I | HOH270 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA J 210 |
| Chain | Residue |
| J | ASP32 |
| J | ASP34 |
| J | ASP125 |
| J | PO4211 |
| J | HOH309 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA K 211 |
| Chain | Residue |
| K | ASP32 |
| K | ASP34 |
| K | ASP125 |
| K | PO4212 |
| K | HOH213 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA L 212 |
| Chain | Residue |
| L | ASP32 |
| L | ASP34 |
| L | ASP125 |
| L | PO4213 |
| L | HOH215 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA M 213 |
| Chain | Residue |
| M | ASP32 |
| M | ASP34 |
| M | ASP125 |
| M | PO4214 |
| M | HOH277 |
| M | HOH329 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA N 214 |
| Chain | Residue |
| M | HOH221 |
| N | ASP32 |
| N | ASP34 |
| N | ASP125 |
| N | PO4215 |
| N | HOH217 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA O 215 |
| Chain | Residue |
| O | ASP32 |
| O | ASP34 |
| O | ASP125 |
| O | PO4216 |
| O | HOH221 |
| O | HOH222 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA P 216 |
| Chain | Residue |
| P | ASP32 |
| P | ASP34 |
| P | ASP125 |
| P | PO4217 |
| P | HOH218 |
| P | HOH299 |
| site_id | BC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 202 |
| Chain | Residue |
| A | CA201 |
| A | HOH203 |
| A | HOH204 |
| A | HOH205 |
| D | SER187 |
| A | ASP32 |
| A | VAL33 |
| A | ASP34 |
| A | THR76 |
| A | GLY77 |
| A | LYS102 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 203 |
| Chain | Residue |
| A | SER187 |
| B | ASP32 |
| B | VAL33 |
| B | ASP34 |
| B | THR76 |
| B | GLY77 |
| B | LYS102 |
| B | CA202 |
| B | HOH206 |
| site_id | CC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 C 204 |
| Chain | Residue |
| B | SER187 |
| B | HOH207 |
| C | ASP32 |
| C | VAL33 |
| C | ASP34 |
| C | THR76 |
| C | GLY77 |
| C | LYS102 |
| C | CA203 |
| C | HOH205 |
| C | HOH206 |
| site_id | CC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 D 205 |
| Chain | Residue |
| C | SER187 |
| D | ASP32 |
| D | VAL33 |
| D | ASP34 |
| D | THR76 |
| D | GLY77 |
| D | LYS102 |
| D | CA204 |
| D | HOH209 |
| D | HOH210 |
| site_id | CC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 E 206 |
| Chain | Residue |
| E | ASP32 |
| E | VAL33 |
| E | ASP34 |
| E | THR76 |
| E | GLY77 |
| E | LYS102 |
| E | CA205 |
| E | HOH208 |
| E | HOH209 |
| H | SER187 |
| site_id | CC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 F 207 |
| Chain | Residue |
| F | ASP32 |
| F | VAL33 |
| F | ASP34 |
| F | THR76 |
| F | GLY77 |
| F | LYS102 |
| F | CA206 |
| F | HOH238 |
| F | HOH374 |
| site_id | CC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PO4 G 208 |
| Chain | Residue |
| F | SER187 |
| G | ASP32 |
| G | VAL33 |
| G | ASP34 |
| G | THR76 |
| G | GLY77 |
| G | ARG78 |
| G | LYS102 |
| G | CA207 |
| G | HOH210 |
| G | HOH211 |
| G | HOH400 |
| site_id | CC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 H 209 |
| Chain | Residue |
| G | SER187 |
| H | ASP32 |
| H | VAL33 |
| H | ASP34 |
| H | THR76 |
| H | GLY77 |
| H | LYS102 |
| H | CA208 |
| H | HOH212 |
| site_id | CC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 I 210 |
| Chain | Residue |
| I | ASP32 |
| I | VAL33 |
| I | ASP34 |
| I | THR76 |
| I | GLY77 |
| I | ARG78 |
| I | LYS102 |
| I | CA209 |
| I | HOH270 |
| L | SER187 |
| site_id | CC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 J 211 |
| Chain | Residue |
| I | SER187 |
| J | ASP32 |
| J | VAL33 |
| J | ASP34 |
| J | THR76 |
| J | GLY77 |
| J | ARG78 |
| J | LYS102 |
| J | CA210 |
| J | HOH212 |
| site_id | CC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 K 212 |
| Chain | Residue |
| J | SER187 |
| K | ASP32 |
| K | VAL33 |
| K | ASP34 |
| K | THR76 |
| K | GLY77 |
| K | ARG78 |
| K | LYS102 |
| K | CA211 |
| K | HOH294 |
| site_id | DC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 L 213 |
| Chain | Residue |
| K | SER187 |
| L | ASP32 |
| L | VAL33 |
| L | ASP34 |
| L | THR76 |
| L | GLY77 |
| L | LYS102 |
| L | CA212 |
| L | HOH214 |
| site_id | DC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 M 214 |
| Chain | Residue |
| M | ASP32 |
| M | VAL33 |
| M | ASP34 |
| M | THR76 |
| M | GLY77 |
| M | ARG78 |
| M | LYS102 |
| M | CA213 |
| M | HOH329 |
| site_id | DC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 N 215 |
| Chain | Residue |
| M | SER187 |
| M | HOH221 |
| N | ASP32 |
| N | VAL33 |
| N | ASP34 |
| N | THR76 |
| N | GLY77 |
| N | ARG78 |
| N | LYS102 |
| N | CA214 |
| N | HOH218 |
| site_id | DC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 O 216 |
| Chain | Residue |
| O | ASP32 |
| O | VAL33 |
| O | ASP34 |
| O | THR76 |
| O | GLY77 |
| O | ARG78 |
| O | LYS102 |
| O | CA215 |
| O | HOH221 |
| O | HOH223 |
| site_id | DC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 P 217 |
| Chain | Residue |
| P | ASP32 |
| P | VAL33 |
| P | ASP34 |
| P | THR76 |
| P | GLY77 |
| P | ARG78 |
| P | LYS102 |
| P | CA216 |
| P | HOH299 |
| P | HOH329 |
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 |
