1JKX
Unexpected formation of an epoxide-derived multisubstrate adduct inhibitor on the active site of GAR transformylase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0006974 | biological_process | DNA damage response |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0006974 | biological_process | DNA damage response |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006164 | biological_process | purine nucleotide biosynthetic process |
| C | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| C | 0006974 | biological_process | DNA damage response |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006164 | biological_process | purine nucleotide biosynthetic process |
| D | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| D | 0006974 | biological_process | DNA damage response |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE 138 A 1221 |
| Chain | Residue |
| A | ASN10 |
| A | ILE91 |
| A | LEU92 |
| A | VAL97 |
| A | ILE107 |
| A | HIS108 |
| A | PRO109 |
| A | VAL139 |
| A | GLN170 |
| A | GLU173 |
| A | HOH1222 |
| A | GLY11 |
| A | HOH1223 |
| A | HOH1230 |
| A | HOH1233 |
| A | HOH1236 |
| A | HOH1238 |
| A | HOH1240 |
| A | HOH1241 |
| A | HOH1242 |
| A | HOH1308 |
| A | HOH1320 |
| A | SER12 |
| A | HOH1330 |
| A | HOH1344 |
| A | HOH1387 |
| C | LYS153 |
| A | ASN13 |
| A | ARG64 |
| A | GLY87 |
| A | PHE88 |
| A | MET89 |
| A | ARG90 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE 138 B 2221 |
| Chain | Residue |
| B | ASN10 |
| B | GLY11 |
| B | SER12 |
| B | ASN13 |
| B | LYS37 |
| B | ARG64 |
| B | GLY87 |
| B | PHE88 |
| B | MET89 |
| B | ARG90 |
| B | ILE91 |
| B | LEU92 |
| B | VAL97 |
| B | ILE107 |
| B | HIS108 |
| B | PRO109 |
| B | VAL139 |
| B | GLU173 |
| B | HOH2227 |
| B | HOH2231 |
| B | HOH2233 |
| B | HOH2240 |
| B | HOH2246 |
| B | HOH2251 |
| B | HOH2255 |
| B | HOH2266 |
| B | HOH2278 |
| B | HOH2288 |
| B | HOH2307 |
| B | HOH2342 |
| B | HOH2384 |
| D | GLU131 |
| D | LYS153 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE 138 C 3221 |
| Chain | Residue |
| C | ASN10 |
| C | GLY11 |
| C | SER12 |
| C | ASN13 |
| C | ARG64 |
| C | GLY87 |
| C | PHE88 |
| C | MET89 |
| C | ARG90 |
| C | ILE91 |
| C | LEU92 |
| C | VAL97 |
| C | ILE107 |
| C | HIS108 |
| C | PRO109 |
| C | VAL139 |
| C | GLN170 |
| C | GLU173 |
| C | HOH3224 |
| C | HOH3234 |
| C | HOH3248 |
| C | HOH3259 |
| C | HOH3266 |
| C | HOH3270 |
| C | HOH3280 |
| C | HOH3286 |
| C | HOH3292 |
| C | HOH3319 |
| C | HOH3339 |
| C | HOH3365 |
| C | HOH3366 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE 138 D 4221 |
| Chain | Residue |
| D | GLY11 |
| D | SER12 |
| D | ASN13 |
| D | ARG64 |
| D | GLY87 |
| D | PHE88 |
| D | MET89 |
| D | ARG90 |
| D | ILE91 |
| D | LEU92 |
| D | VAL97 |
| D | ILE107 |
| D | HIS108 |
| D | PRO109 |
| D | VAL139 |
| D | GLU173 |
| D | HOH4224 |
| D | HOH4227 |
| D | HOH4230 |
| D | HOH4237 |
| D | HOH4261 |
| D | HOH4262 |
| D | HOH4277 |
| D | HOH4283 |
| D | HOH4326 |
| D | HOH4327 |
| D | HOH4328 |
| B | GLU131 |
| D | ASN10 |
Functional Information from PROSITE/UniProt
| site_id | PS00373 |
| Number of Residues | 24 |
| Details | GART Phosphoribosylglycinamide formyltransferase active site. GtSVhFVtDeLDgGpvIlqakvpV |
| Chain | Residue | Details |
| A | GLY133-VAL156 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10433709 |
| Chain | Residue | Details |
| A | HIS108 | |
| B | HIS108 | |
| C | HIS108 | |
| D | HIS108 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 |
| Chain | Residue | Details |
| A | GLY11 | |
| A | MET89 | |
| B | GLY11 | |
| B | MET89 | |
| C | GLY11 | |
| C | MET89 | |
| D | GLY11 | |
| D | MET89 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510 |
| Chain | Residue | Details |
| A | ARG64 | |
| A | ASN106 | |
| B | ARG64 | |
| B | ASN106 | |
| C | ARG64 | |
| C | ASN106 | |
| D | ARG64 | |
| D | ASN106 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 |
| Chain | Residue | Details |
| A | THR140 | |
| A | GLN170 | |
| B | THR140 | |
| B | GLN170 | |
| C | THR140 | |
| C | GLN170 | |
| D | THR140 | |
| D | GLN170 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Raises pKa of active site His => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10433709 |
| Chain | Residue | Details |
| A | ASP144 | |
| B | ASP144 | |
| C | ASP144 | |
| D | ASP144 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| A | SER135 | |
| A | ASN106 | |
| A | ASP144 | |
| A | HIS108 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| B | ASP144 | |
| B | HIS108 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| C | ASP144 | |
| C | HIS108 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| D | ASP144 | |
| D | HIS108 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| B | SER135 | |
| B | ASN106 | |
| B | ASP144 | |
| B | HIS108 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| C | SER135 | |
| C | ASN106 | |
| C | ASP144 | |
| C | HIS108 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| D | SER135 | |
| D | ASN106 | |
| D | ASP144 | |
| D | HIS108 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| A | ASN106 | |
| A | ASP144 | |
| A | HIS108 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| B | ASN106 | |
| B | ASP144 | |
| B | HIS108 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| C | ASN106 | |
| C | ASP144 | |
| C | HIS108 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| D | ASN106 | |
| D | ASP144 | |
| D | HIS108 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| A | ASP144 | |
| A | HIS108 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 363 |
| Chain | Residue | Details |
| A | ASN106 | electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| A | HIS108 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| A | SER135 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | ASP144 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 363 |
| Chain | Residue | Details |
| B | ASN106 | electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| B | HIS108 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| B | SER135 | electrostatic stabiliser, hydrogen bond donor, steric role |
| B | ASP144 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 363 |
| Chain | Residue | Details |
| C | ASN106 | electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| C | HIS108 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| C | SER135 | electrostatic stabiliser, hydrogen bond donor, steric role |
| C | ASP144 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 363 |
| Chain | Residue | Details |
| D | ASN106 | electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| D | HIS108 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| D | SER135 | electrostatic stabiliser, hydrogen bond donor, steric role |
| D | ASP144 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity |
