1KJJ
Crystal structure of glycniamide ribonucleotide transformylase in complex with Mg-ATP-gamma-S
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0000166 | molecular_function | nucleotide 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 | AGS1 |
| A | GLU279 |
| A | HOH627 |
| A | HOH736 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 394 |
| Chain | Residue |
| A | AGS1 |
| A | GLU267 |
| A | GLU279 |
| A | HOH467 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 393 |
| Chain | Residue |
| B | AGS395 |
| B | HOH479 |
| B | HOH626 |
| B | GLU279 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 394 |
| Chain | Residue |
| B | GLU267 |
| B | GLU279 |
| B | AGS395 |
| B | HOH527 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 395 |
| Chain | Residue |
| A | ASN100 |
| A | VAL101 |
| A | PRO103 |
| A | HOH432 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 396 |
| Chain | Residue |
| A | ARG43 |
| A | VAL58 |
| A | ARG119 |
| A | PHE134 |
| A | HOH741 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE AGS A 1 |
| Chain | Residue |
| A | ARG114 |
| A | SER130 |
| A | ILE153 |
| A | LYS155 |
| A | SER160 |
| A | SER161 |
| A | GLY162 |
| A | GLN165 |
| A | GLU195 |
| A | GLY196 |
| A | VAL198 |
| A | GLU203 |
| A | GLN225 |
| A | GLU267 |
| A | PHE269 |
| A | GLU279 |
| A | MG393 |
| A | MG394 |
| A | HOH467 |
| A | HOH471 |
| A | HOH495 |
| A | HOH497 |
| A | HOH514 |
| A | HOH617 |
| A | HOH702 |
| A | HOH736 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE AGS B 395 |
| Chain | Residue |
| B | ARG114 |
| B | LYS155 |
| B | SER159 |
| B | SER160 |
| B | SER161 |
| B | GLY162 |
| B | GLN165 |
| B | GLU195 |
| B | VAL197 |
| B | VAL198 |
| B | GLU203 |
| B | GLU267 |
| B | GLU279 |
| B | MG393 |
| B | MG394 |
| B | HOH461 |
| B | HOH527 |
| B | HOH626 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MPO A 397 |
| Chain | Residue |
| A | ASP46 |
| A | MET50 |
| A | HIS51 |
| A | ARG55 |
| A | SER56 |
| A | GLU143 |
| A | HOH402 |
| A | HOH465 |
| A | HOH523 |
| B | LEU8 |
| B | HIS54 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01643","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10913290","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11953435","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 | 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 | 7 |
| 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 |
| B | ARG363 | electrostatic stabiliser, hydrogen bond donor |
