1KJ8
Crystal Structure of PurT-Encoded Glycinamide Ribonucleotide Transformylase in Complex with Mg-ATP 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 | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 393 |
| Chain | Residue |
| A | ATP1 |
| A | GLU279 |
| A | HOH410 |
| A | HOH533 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 394 |
| Chain | Residue |
| A | ATP1 |
| A | GLU267 |
| A | GLU279 |
| A | HOH404 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 393 |
| Chain | Residue |
| B | ATP397 |
| B | HOH684 |
| B | GLU279 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 394 |
| Chain | Residue |
| B | GLU267 |
| B | GLU279 |
| B | ATP397 |
| B | HOH605 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 395 |
| Chain | Residue |
| A | ASN100 |
| A | VAL101 |
| A | PRO103 |
| A | HOH797 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 395 |
| Chain | Residue |
| B | ASN100 |
| B | VAL101 |
| B | PRO103 |
| B | HOH493 |
| B | HOH540 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 396 |
| Chain | Residue |
| A | GLU84 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 397 |
| Chain | Residue |
| A | GLN341 |
| A | VAL374 |
| A | HOH725 |
| A | HOH732 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 396 |
| Chain | Residue |
| B | HIS216 |
| B | PHE217 |
| B | HOH500 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 398 |
| Chain | Residue |
| A | ARG33 |
| A | HOH509 |
| B | ARG33 |
| B | EDO399 |
| site_id | BC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE ATP A 1 |
| Chain | Residue |
| A | ARG114 |
| A | ILE153 |
| A | LYS155 |
| A | SER160 |
| A | SER161 |
| A | GLY162 |
| A | GLN165 |
| A | GLU195 |
| A | GLY196 |
| A | VAL198 |
| A | PHE200 |
| A | GLU203 |
| A | GLN225 |
| A | GLY228 |
| A | GLU267 |
| A | PHE269 |
| A | GLU279 |
| A | MG393 |
| A | MG394 |
| A | GAR399 |
| A | HOH402 |
| A | HOH404 |
| A | HOH410 |
| A | HOH455 |
| A | HOH462 |
| A | HOH479 |
| A | HOH527 |
| A | HOH533 |
| A | HOH619 |
| A | HOH770 |
| A | HOH901 |
| site_id | BC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP B 397 |
| Chain | Residue |
| B | ARG114 |
| B | LYS155 |
| B | SER159 |
| B | SER160 |
| B | SER161 |
| B | GLY162 |
| B | GLN165 |
| B | GLU195 |
| B | VAL198 |
| B | GLU203 |
| B | GLU267 |
| B | PHE269 |
| B | GLU279 |
| B | MG393 |
| B | MG394 |
| B | HOH489 |
| B | HOH511 |
| B | HOH605 |
| site_id | BC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE GAR A 399 |
| Chain | Residue |
| A | HOH421 |
| A | HOH433 |
| A | HOH441 |
| A | HOH446 |
| A | HOH513 |
| A | HOH517 |
| A | HOH551 |
| A | HOH574 |
| A | ATP1 |
| A | GLY21 |
| A | GLU22 |
| A | LEU23 |
| A | GLU82 |
| A | ILE83 |
| A | SER160 |
| A | SER161 |
| A | ASP286 |
| A | LYS355 |
| A | ARG362 |
| A | ARG363 |
| A | HOH405 |
| A | HOH413 |
| site_id | BC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE GAR B 398 |
| Chain | Residue |
| B | GLY21 |
| B | GLU22 |
| B | LEU23 |
| B | GLU82 |
| B | ILE83 |
| B | ASP286 |
| B | LYS355 |
| B | ARG362 |
| B | ARG363 |
| B | HOH404 |
| B | HOH411 |
| B | HOH423 |
| B | HOH435 |
| B | HOH495 |
| B | HOH607 |
| B | HOH651 |
| site_id | BC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE MPO A 400 |
| Chain | Residue |
| A | ASP46 |
| A | MET50 |
| A | HIS51 |
| A | ARG55 |
| A | SER56 |
| A | GLU143 |
| A | HOH460 |
| A | HOH476 |
| A | HOH552 |
| A | HOH832 |
| A | HOH871 |
| B | LEU8 |
| B | HIS54 |
| site_id | BC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO B 399 |
| Chain | Residue |
| A | CL398 |
| B | GLU30 |
| B | ARG33 |
| B | ASP296 |
| B | LEU297 |
| B | SER298 |
| B | ALA301 |
| B | HOH440 |
| B | HOH453 |
| B | HOH614 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 400 |
| Chain | Residue |
| B | SER240 |
| B | PRO241 |
| B | LEU242 |
| B | HOH642 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 401 |
| Chain | Residue |
| A | ARG106 |
| A | LYS109 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01643, ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435 |
| Chain | Residue | Details |
| A | LEU23 | |
| A | THR287 | |
| A | PRO356 | |
| A | ARG363 | |
| B | LEU23 | |
| B | ILE83 | |
| B | GLU115 | |
| B | PRO156 | |
| B | SER161 | |
| B | GLY196 | |
| B | ILE204 | |
| A | ILE83 | |
| B | LEU268 | |
| B | VAL280 | |
| B | THR287 | |
| B | PRO356 | |
| B | ARG363 | |
| A | GLU115 | |
| A | PRO156 | |
| A | SER161 | |
| A | GLY196 | |
| A | ILE204 | |
| A | LEU268 | |
| A | VAL280 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | TYR180 | |
| B | TYR180 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ez1 |
| Chain | Residue | Details |
| A | ASP286 | |
| A | ARG362 | |
| A | THR287 | |
| A | SER160 | |
| A | GLY162 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ez1 |
| 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 | SER161 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS163 | electrostatic stabiliser, hydrogen bond donor |
| A | LEU268 | electrostatic stabiliser, metal ligand |
| A | VAL280 | electrostatic stabiliser, metal ligand |
| A | THR287 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| A | GLY288 | electrostatic stabiliser, hydrogen bond donor |
| A | LEU364 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 665 |
| Chain | Residue | Details |
| B | SER161 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS163 | electrostatic stabiliser, hydrogen bond donor |
| B | LEU268 | electrostatic stabiliser, metal ligand |
| B | VAL280 | electrostatic stabiliser, metal ligand |
| B | THR287 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| B | GLY288 | electrostatic stabiliser, hydrogen bond donor |
| B | LEU364 | electrostatic stabiliser, hydrogen bond donor |
