3DCJ
Crystal structure of glycinamide formyltransferase (PurN) from Mycobacterium tuberculosis in complex with 5-methyl-5,6,7,8-tetrahydrofolic acid derivative
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| 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 | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046653 | biological_process | tetrahydrofolate metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| 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 | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046653 | biological_process | tetrahydrofolate metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE THH A 401 |
| Chain | Residue |
| A | PHE98 |
| A | GLY152 |
| A | THR153 |
| A | ASP154 |
| A | MG301 |
| A | HOH468 |
| A | HOH513 |
| A | MET99 |
| A | ARG100 |
| A | ILE101 |
| A | LEU102 |
| A | ASN116 |
| A | THR128 |
| A | VAL149 |
| A | ASP150 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | THR117 |
| A | THH401 |
| A | HOH423 |
| A | HOH491 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 302 |
| Chain | Residue |
| A | PRO165 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE THH B 401 |
| Chain | Residue |
| B | PHE98 |
| B | ARG100 |
| B | ILE101 |
| B | LEU102 |
| B | ASN116 |
| B | VAL149 |
| B | ASP150 |
| B | GLY152 |
| B | HOH582 |
| B | HOH649 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NO3 B 301 |
| Chain | Residue |
| A | LEU68 |
| A | ALA69 |
| B | ALA86 |
| B | PRO90 |
| B | ARG109 |
| B | PHE110 |
| B | ARG113 |
| B | HOH647 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 302 |
| Chain | Residue |
| B | PRO165 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01930 |
| Chain | Residue | Details |
| A | HIS118 | |
| B | HIS118 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01930 |
| Chain | Residue | Details |
| A | ARG74 | |
| B | ARG74 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN116 | |
| B | ARG100 | |
| B | ASN116 | |
| B | THR117 | |
| B | ASP150 | |
| A | ARG100 | |
| A | THR117 | |
| A | ASP150 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Raises pKa of active site His => ECO:0000255|HAMAP-Rule:MF_01930 |
| Chain | Residue | Details |
| A | ASP154 | |
| B | ASP154 |
