1B93
METHYLGLYOXAL SYNTHASE FROM ESCHERICHIA COLI
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 301 |
| Chain | Residue |
| B | LYS23 |
| B | THR45 |
| B | THR47 |
| B | THR48 |
| B | SER65 |
| B | GLY66 |
| B | ARG150 |
| B | FMT204 |
| B | HOH472 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 201 |
| Chain | Residue |
| A | HIS19 |
| A | GLY66 |
| A | ASP71 |
| A | PHE88 |
| A | HIS98 |
| A | FMT202 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 202 |
| Chain | Residue |
| A | ALA18 |
| A | THR45 |
| A | SER65 |
| A | GLY66 |
| A | FMT201 |
| A | FMT203 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT A 203 |
| Chain | Residue |
| A | LEU16 |
| A | VAL17 |
| A | ALA18 |
| A | LYS23 |
| A | THR45 |
| A | THR48 |
| A | FMT202 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT B 204 |
| Chain | Residue |
| B | VAL17 |
| B | HIS19 |
| B | ASP71 |
| B | PHE88 |
| B | HIS98 |
| B | PO4301 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FMT C 205 |
| Chain | Residue |
| C | VAL17 |
| C | HIS19 |
| C | GLY66 |
| C | ASP71 |
| C | PHE88 |
| C | HIS98 |
| C | FMT206 |
| C | HOH518 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT C 206 |
| Chain | Residue |
| C | LYS23 |
| C | THR45 |
| C | SER65 |
| C | GLY66 |
| C | FMT205 |
| C | FMT207 |
| C | HOH540 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT C 207 |
| Chain | Residue |
| C | LEU16 |
| C | VAL17 |
| C | ALA18 |
| C | LYS23 |
| C | THR45 |
| C | THR48 |
| C | FMT206 |
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 | 3 |
| 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 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| 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 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| 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 | |
| A | THR45 | |
| A | SER65 | |
| B | LYS23 | |
| B | THR45 | |
| B | SER65 | |
| C | LYS23 | |
| C | THR45 | |
| C | SER65 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| 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 | HIS98 | |
| B | HIS98 | |
| C | HIS98 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 10715115, 10368300 |
| Chain | Residue | Details |
| A | HIS98 | |
| A | ASP71 | |
| A | HIS19 | |
| A | ASP101 | |
| A | ASP91 | |
| A | GLY66 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 10715115, 10368300 |
| Chain | Residue | Details |
| B | HIS98 | |
| B | ASP71 | |
| B | HIS19 | |
| B | ASP101 | |
| B | ASP91 | |
| B | GLY66 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 10715115, 10368300 |
| Chain | Residue | Details |
| C | HIS98 | |
| C | ASP71 | |
| C | HIS19 | |
| C | ASP101 | |
| C | ASP91 | |
| C | GLY66 |
| 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 | HIS98 | 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 | HIS98 | 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 | HIS98 | 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 |
