1RLM
Crystal Structure of ybiV from Escherichia coli K12
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050286 | molecular_function | sorbitol-6-phosphatase activity |
| A | 0050308 | molecular_function | sugar-phosphatase activity |
| A | 0103026 | molecular_function | fructose-1-phosphatase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050286 | molecular_function | sorbitol-6-phosphatase activity |
| B | 0050308 | molecular_function | sugar-phosphatase activity |
| B | 0103026 | molecular_function | fructose-1-phosphatase activity |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016791 | molecular_function | phosphatase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050286 | molecular_function | sorbitol-6-phosphatase activity |
| C | 0050308 | molecular_function | sugar-phosphatase activity |
| C | 0103026 | molecular_function | fructose-1-phosphatase activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016791 | molecular_function | phosphatase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050286 | molecular_function | sorbitol-6-phosphatase activity |
| D | 0050308 | molecular_function | sugar-phosphatase activity |
| D | 0103026 | molecular_function | fructose-1-phosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 800 |
| Chain | Residue |
| A | ASP9 |
| A | ASP11 |
| A | ASP215 |
| A | SER216 |
| A | HOH926 |
| A | HOH946 |
| A | HOH949 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 801 |
| Chain | Residue |
| B | ASP215 |
| B | SER216 |
| B | HOH828 |
| B | HOH858 |
| B | ASP9 |
| B | ASP11 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 802 |
| Chain | Residue |
| D | ASP9 |
| D | ASP11 |
| D | ASP215 |
| D | SER216 |
| D | HOH972 |
| D | HOH976 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 803 |
| Chain | Residue |
| C | ASP9 |
| C | ASP11 |
| C | ASP215 |
| C | SER216 |
| C | HOH832 |
| C | HOH912 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 804 |
| Chain | Residue |
| A | GLY45 |
| A | ASN46 |
| A | MET126 |
| A | HIS129 |
| A | TYR130 |
| A | SER150 |
| A | SER178 |
| A | ASP184 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 806 |
| Chain | Residue |
| A | LYS19 |
| A | LEU125 |
| A | LYS128 |
| A | HIS129 |
| A | HOH904 |
| A | HOH944 |
| A | HOH947 |
| A | HOH950 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 807 |
| Chain | Residue |
| B | GLY45 |
| B | ASN46 |
| B | ASN68 |
| B | TYR130 |
| B | SER150 |
| B | SER178 |
| B | ASP184 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 808 |
| Chain | Residue |
| C | GLY45 |
| C | HIS129 |
| C | TYR130 |
| C | SER150 |
| C | SER178 |
| C | ASP184 |
| C | GOL809 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL C 809 |
| Chain | Residue |
| C | ASP9 |
| C | MET10 |
| C | ASP11 |
| C | SER44 |
| C | GLY45 |
| C | ASN46 |
| C | LYS192 |
| C | ASN218 |
| C | GOL808 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 810 |
| Chain | Residue |
| D | GLY45 |
| D | MET126 |
| D | TYR130 |
| D | SER150 |
| D | SER178 |
| D | ASP184 |
| D | HOH914 |
Functional Information from PROSITE/UniProt
| site_id | PS01229 |
| Number of Residues | 23 |
| Details | COF_2 Hypothetical cof family signature 2. IGDSgNDaemLkmArySfaMgnA |
| Chain | Residue | Details |
| A | ILE213-ALA235 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000255 |
| Chain | Residue | Details |
| A | ASP9 | |
| B | ASP9 | |
| C | ASP9 | |
| D | ASP9 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP9 | |
| B | ASP11 | |
| B | SER44 | |
| B | LYS192 | |
| B | ASP215 | |
| B | SER216 | |
| C | ASP9 | |
| C | MET10 | |
| C | ASP11 | |
| C | SER44 | |
| C | LYS192 | |
| A | MET10 | |
| C | ASP215 | |
| C | SER216 | |
| D | ASP9 | |
| D | MET10 | |
| D | ASP11 | |
| D | SER44 | |
| D | LYS192 | |
| D | ASP215 | |
| D | SER216 | |
| A | ASP11 | |
| A | SER44 | |
| A | LYS192 | |
| A | ASP215 | |
| A | SER216 | |
| B | ASP9 | |
| B | MET10 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ASN218 | |
| B | ASN218 | |
| C | ASN218 | |
| D | ASN218 |
