1EZ1
STRUCTURE OF ESCHERICHIA COLI PURT-ENCODED GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE COMPLEXED WITH MG, AMPPNP, AND GAR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0008776 | molecular_function | acetate kinase activity |
| A | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| A | 0016742 | molecular_function | hydroxymethyl-, formyl- and related transferase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0043815 | molecular_function | phosphoribosylglycinamide formyltransferase 2 activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0008776 | molecular_function | acetate kinase activity |
| B | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| B | 0016742 | molecular_function | hydroxymethyl-, formyl- and related transferase activity |
| B | 0016874 | molecular_function | ligase activity |
| B | 0043815 | molecular_function | phosphoribosylglycinamide formyltransferase 2 activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | SER160 |
| A | GLU279 |
| A | ANP400 |
| A | HOH1164 |
| A | HOH1251 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 402 |
| Chain | Residue |
| A | GLU267 |
| A | GLU279 |
| A | ANP400 |
| A | HOH1106 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | GLU279 |
| B | ANP1003 |
| B | HOH1616 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 402 |
| Chain | Residue |
| B | GLU267 |
| B | GLU279 |
| B | ANP1003 |
| B | HOH2183 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 960 |
| Chain | Residue |
| A | THR2 |
| A | HOH1252 |
| A | HOH1981 |
| A | HOH1982 |
| B | GLN341 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT B 961 |
| Chain | Residue |
| B | HOH2223 |
| B | HOH2231 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1001 |
| Chain | Residue |
| A | ASN100 |
| A | VAL101 |
| A | PRO103 |
| A | HOH1189 |
| A | HOH1670 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 1002 |
| Chain | Residue |
| B | ASN100 |
| B | VAL101 |
| B | PRO103 |
| B | HOH1453 |
| B | HOH1930 |
| site_id | AC9 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ANP A 400 |
| Chain | Residue |
| A | ARG114 |
| A | ILE153 |
| A | LYS155 |
| A | SER160 |
| A | SER161 |
| A | GLY162 |
| A | GLN165 |
| A | GLU195 |
| A | GLY196 |
| A | VAL197 |
| A | VAL198 |
| A | PHE200 |
| A | GLU203 |
| A | GLN225 |
| A | GLU267 |
| A | PHE269 |
| A | GLU279 |
| A | MG401 |
| A | MG402 |
| A | GAR410 |
| A | HOH1106 |
| A | HOH1164 |
| A | HOH1203 |
| A | HOH1234 |
| A | HOH1251 |
| A | HOH1391 |
| A | HOH1515 |
| A | HOH1695 |
| site_id | BC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE GAR A 410 |
| Chain | Residue |
| A | GLY21 |
| A | GLU22 |
| A | LEU23 |
| A | GLU82 |
| A | ILE83 |
| A | SER161 |
| A | ASP286 |
| A | LYS355 |
| A | ARG362 |
| A | ARG363 |
| A | ANP400 |
| A | HOH1104 |
| A | HOH1140 |
| A | HOH1153 |
| A | HOH1177 |
| A | HOH1226 |
| A | HOH1284 |
| A | HOH1295 |
| A | HOH1571 |
| A | HOH1934 |
| site_id | BC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ANP B 1003 |
| Chain | Residue |
| B | HOH1324 |
| B | HOH1337 |
| B | HOH1469 |
| B | HOH2183 |
| B | ARG114 |
| B | SER130 |
| B | LYS155 |
| B | SER159 |
| B | SER160 |
| B | SER161 |
| B | GLY162 |
| B | GLN165 |
| B | GLU195 |
| B | VAL197 |
| B | VAL198 |
| B | PHE200 |
| B | GLU203 |
| B | GLU267 |
| B | PHE269 |
| B | GLU279 |
| B | MG401 |
| B | MG402 |
| site_id | BC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE GAR B 411 |
| Chain | Residue |
| B | GLY21 |
| B | GLU22 |
| B | LEU23 |
| B | GLU82 |
| B | ILE83 |
| B | ASP286 |
| B | LYS355 |
| B | ARG362 |
| B | ARG363 |
| B | HOH1111 |
| B | HOH1132 |
| B | HOH1149 |
| B | HOH1195 |
| B | HOH1419 |
| B | HOH1768 |
| B | HOH1806 |
| B | HOH1912 |
| B | HOH1927 |
| site_id | BC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MPO A 950 |
| Chain | Residue |
| A | ASP46 |
| A | MET50 |
| A | HIS51 |
| A | ARG55 |
| A | SER56 |
| A | GLU143 |
| A | HOH1187 |
| A | HOH1206 |
| A | HOH1297 |
| A | HOH1473 |
| A | HOH1569 |
| A | HOH1635 |
| B | LEU8 |
| B | HIS54 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01643, ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435 |
| Chain | Residue | Details |
| A | GLU22 | |
| A | ASP286 | |
| A | LYS355 | |
| A | ARG362 | |
| B | GLU22 | |
| B | GLU82 | |
| B | ARG114 | |
| B | LYS155 | |
| B | SER160 | |
| B | GLU195 | |
| B | GLU203 | |
| A | GLU82 | |
| B | GLU267 | |
| B | GLU279 | |
| B | ASP286 | |
| A | ARG114 | |
| A | LYS155 | |
| A | SER160 | |
| A | GLU195 | |
| A | GLU203 | |
| A | GLU267 | |
| A | GLU279 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS179 | |
| B | LYS179 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 10913290, 11953435 |
| Chain | Residue | Details |
| A | ASP286 | |
| A | ARG362 | |
| A | THR287 | |
| A | SER160 | |
| A | GLY162 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 10913290, 11953435 |
| Chain | Residue | Details |
| B | ASP286 | |
| B | ARG362 | |
| B | THR287 | |
| B | SER160 | |
| B | GLY162 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 665 |
| Chain | Residue | Details |
| A | SER160 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY162 | electrostatic stabiliser, hydrogen bond donor |
| A | GLU267 | electrostatic stabiliser, metal ligand |
| A | GLU279 | electrostatic stabiliser, metal ligand |
| A | ASP286 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| A | THR287 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG363 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 665 |
| Chain | Residue | Details |
| B | SER160 | electrostatic stabiliser, hydrogen bond donor |
| B | GLY162 | electrostatic stabiliser, hydrogen bond donor |
| B | GLU267 | electrostatic stabiliser, metal ligand |
| B | GLU279 | electrostatic stabiliser, metal ligand |
| B | ASP286 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| B | THR287 | electrostatic stabiliser, hydrogen bond donor |
