1S8A
H98Q Mutant of Methylglyoxal Synthase from E. coli complexed with Phosphoglycolic Acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008929 | molecular_function | methylglyoxal synthase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019242 | biological_process | methylglyoxal biosynthetic process |
| A | 0034214 | biological_process | protein hexamerization |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008929 | molecular_function | methylglyoxal synthase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019242 | biological_process | methylglyoxal biosynthetic process |
| B | 0034214 | biological_process | protein hexamerization |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008929 | molecular_function | methylglyoxal synthase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019242 | biological_process | methylglyoxal biosynthetic process |
| C | 0034214 | biological_process | protein hexamerization |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008929 | molecular_function | methylglyoxal synthase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019242 | biological_process | methylglyoxal biosynthetic process |
| D | 0034214 | biological_process | protein hexamerization |
| D | 0042802 | molecular_function | identical protein binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0008929 | molecular_function | methylglyoxal synthase activity |
| E | 0016829 | molecular_function | lyase activity |
| E | 0019242 | biological_process | methylglyoxal biosynthetic process |
| E | 0034214 | biological_process | protein hexamerization |
| E | 0042802 | molecular_function | identical protein binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0008929 | molecular_function | methylglyoxal synthase activity |
| F | 0016829 | molecular_function | lyase activity |
| F | 0019242 | biological_process | methylglyoxal biosynthetic process |
| F | 0034214 | biological_process | protein hexamerization |
| F | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PGA A 201 |
| Chain | Residue |
| A | VAL17 |
| A | ASP71 |
| A | GLN98 |
| A | HOH209 |
| A | HOH216 |
| F | ARG150 |
| A | ALA18 |
| A | LYS23 |
| A | THR45 |
| A | THR47 |
| A | THR48 |
| A | SER65 |
| A | GLY66 |
| A | PRO67 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PGA B 202 |
| Chain | Residue |
| B | VAL17 |
| B | ALA18 |
| B | LYS23 |
| B | THR45 |
| B | THR47 |
| B | THR48 |
| B | SER65 |
| B | GLY66 |
| B | PRO67 |
| B | ASP71 |
| B | HOH218 |
| B | HOH219 |
| E | ARG150 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PGA C 203 |
| Chain | Residue |
| C | VAL17 |
| C | ALA18 |
| C | LYS23 |
| C | THR45 |
| C | THR47 |
| C | THR48 |
| C | SER65 |
| C | GLY66 |
| C | PRO67 |
| C | ASP71 |
| C | GLN98 |
| C | HOH219 |
| D | ARG150 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PGA D 204 |
| Chain | Residue |
| C | ARG150 |
| D | VAL17 |
| D | ALA18 |
| D | LYS23 |
| D | THR45 |
| D | THR47 |
| D | THR48 |
| D | SER65 |
| D | GLY66 |
| D | ASP71 |
| D | GLN98 |
| D | HOH212 |
| D | HOH214 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PGA E 205 |
| Chain | Residue |
| B | ARG150 |
| E | VAL17 |
| E | ALA18 |
| E | LYS23 |
| E | THR45 |
| E | THR47 |
| E | THR48 |
| E | SER65 |
| E | GLY66 |
| E | PRO67 |
| E | ASP71 |
| E | GLN98 |
| E | HOH211 |
| E | HOH221 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PGA F 206 |
| Chain | Residue |
| A | ARG150 |
| F | VAL17 |
| F | ALA18 |
| F | LYS23 |
| F | THR45 |
| F | THR47 |
| F | THR48 |
| F | SER65 |
| F | GLY66 |
| F | PRO67 |
| F | ASP71 |
| F | GLN98 |
| F | HOH217 |
| F | HOH222 |
Functional Information from PROSITE/UniProt
| site_id | PS01335 |
| Number of Residues | 9 |
| Details | METHYLGLYOXAL_SYNTH Methylglyoxal synthase active site. SGPMGGDqQ |
| Chain | Residue | Details |
| A | SER65-GLN73 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00549, ECO:0000269|PubMed:10715115, ECO:0000269|PubMed:11389594, ECO:0000269|PubMed:15049687, ECO:0000269|PubMed:9665712 |
| Chain | Residue | Details |
| A | ASP71 | |
| B | ASP71 | |
| C | ASP71 | |
| D | ASP71 | |
| E | ASP71 | |
| F | ASP71 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00549, ECO:0000269|PubMed:11389594, ECO:0007744|PDB:1IK4 |
| Chain | Residue | Details |
| A | HIS19 | |
| B | HIS19 | |
| C | HIS19 | |
| D | HIS19 | |
| E | HIS19 | |
| F | HIS19 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00549, ECO:0000269|PubMed:10715115, ECO:0000269|PubMed:11389594, ECO:0000269|PubMed:15049687, ECO:0007744|PDB:1EGH, ECO:0007744|PDB:1IK4, ECO:0007744|PDB:1S89, ECO:0007744|PDB:1S8A |
| Chain | Residue | Details |
| A | LYS23 | |
| D | LYS23 | |
| D | THR45 | |
| D | SER65 | |
| E | LYS23 | |
| E | THR45 | |
| E | SER65 | |
| F | LYS23 | |
| F | THR45 | |
| F | SER65 | |
| A | THR45 | |
| A | SER65 | |
| B | LYS23 | |
| B | THR45 | |
| B | SER65 | |
| C | LYS23 | |
| C | THR45 | |
| C | SER65 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00549, ECO:0000269|PubMed:10715115, ECO:0000269|PubMed:11389594, ECO:0007744|PDB:1EGH, ECO:0007744|PDB:1IK4 |
| Chain | Residue | Details |
| A | GLN98 | |
| B | GLN98 | |
| C | GLN98 | |
| D | GLN98 | |
| E | GLN98 | |
| F | GLN98 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 85 |
| Chain | Residue | Details |
| A | HIS19 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLY66 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | ASP71 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASP91 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | GLN98 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASP101 | activator, electrostatic stabiliser, hydrogen bond acceptor, repulsive charge-charge interaction |
| A | ARG107 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 85 |
| Chain | Residue | Details |
| B | HIS19 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLY66 | electrostatic stabiliser, hydrogen bond donor, steric role |
| B | ASP71 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASP91 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| B | GLN98 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASP101 | activator, electrostatic stabiliser, hydrogen bond acceptor, repulsive charge-charge interaction |
| B | ARG107 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 85 |
| Chain | Residue | Details |
| C | HIS19 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | GLY66 | electrostatic stabiliser, hydrogen bond donor, steric role |
| C | ASP71 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | ASP91 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| C | GLN98 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | ASP101 | activator, electrostatic stabiliser, hydrogen bond acceptor, repulsive charge-charge interaction |
| C | ARG107 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 7 |
| Details | M-CSA 85 |
| Chain | Residue | Details |
| D | HIS19 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | GLY66 | electrostatic stabiliser, hydrogen bond donor, steric role |
| D | ASP71 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | ASP91 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| D | GLN98 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | ASP101 | activator, electrostatic stabiliser, hydrogen bond acceptor, repulsive charge-charge interaction |
| D | ARG107 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA5 |
| Number of Residues | 7 |
| Details | M-CSA 85 |
| Chain | Residue | Details |
| E | HIS19 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | GLY66 | electrostatic stabiliser, hydrogen bond donor, steric role |
| E | ASP71 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | ASP91 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| E | GLN98 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | ASP101 | activator, electrostatic stabiliser, hydrogen bond acceptor, repulsive charge-charge interaction |
| E | ARG107 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA6 |
| Number of Residues | 7 |
| Details | M-CSA 85 |
| Chain | Residue | Details |
| F | HIS19 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | GLY66 | electrostatic stabiliser, hydrogen bond donor, steric role |
| F | ASP71 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | ASP91 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| F | GLN98 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | ASP101 | activator, electrostatic stabiliser, hydrogen bond acceptor, repulsive charge-charge interaction |
| F | ARG107 | electrostatic stabiliser, hydrogen bond donor |
