5VYQ
Crystal structure of the N-formyltransferase Rv3404c from mycobacterium tuberculosis in complex with YDP-Qui4N and folinic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004479 | molecular_function | methionyl-tRNA formyltransferase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006413 | biological_process | translational initiation |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016742 | molecular_function | hydroxymethyl-, formyl- and related transferase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0071951 | biological_process | conversion of methionyl-tRNA to N-formyl-methionyl-tRNA |
| B | 0004479 | molecular_function | methionyl-tRNA formyltransferase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006413 | biological_process | translational initiation |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016742 | molecular_function | hydroxymethyl-, formyl- and related transferase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0071951 | biological_process | conversion of methionyl-tRNA to N-formyl-methionyl-tRNA |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue FON A 301 |
| Chain | Residue |
| A | CYS64 |
| A | LEU116 |
| A | ASP117 |
| A | LEU175 |
| A | LYS176 |
| A | 0FX302 |
| A | LI311 |
| A | HOH414 |
| A | HOH425 |
| A | HOH512 |
| A | GLN66 |
| A | ARG67 |
| A | PHE68 |
| A | ASN80 |
| A | TRP92 |
| A | ILE112 |
| A | ASP113 |
| A | GLN115 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue 0FX A 302 |
| Chain | Residue |
| A | ASN10 |
| A | HIS63 |
| A | CYS64 |
| A | LYS65 |
| A | HIS82 |
| A | GLY91 |
| A | PHE93 |
| A | GLN95 |
| A | TYR139 |
| A | HIS205 |
| A | PHE208 |
| A | ASN210 |
| A | FON301 |
| A | LI311 |
| A | HOH425 |
| A | HOH433 |
| A | HOH477 |
| A | HOH486 |
| A | HOH489 |
| A | HOH500 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | SER131 |
| A | GLY194 |
| A | ASN198 |
| A | ARG201 |
| A | HOH430 |
| A | HOH479 |
| B | PHE213 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | VAL225 |
| A | VAL226 |
| A | LEU227 |
| A | HOH488 |
| A | HOH514 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 305 |
| Chain | Residue |
| A | VAL53 |
| A | TYR56 |
| A | HOH434 |
| A | HOH480 |
| A | HOH615 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 306 |
| Chain | Residue |
| A | MET1 |
| A | THR3 |
| A | ASP57 |
| A | HOH614 |
| A | HOH625 |
| A | HOH630 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 307 |
| Chain | Residue |
| A | SER134 |
| A | GLY136 |
| A | ASP206 |
| A | HOH567 |
| A | HOH649 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue EP1 A 308 |
| Chain | Residue |
| A | ASP206 |
| A | ASP207 |
| A | PHE208 |
| A | ARG209 |
| A | HOH432 |
| A | HOH473 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 309 |
| Chain | Residue |
| A | ARG190 |
| A | SER217 |
| B | GLY191 |
| B | HOH622 |
| B | HOH657 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue NA A 310 |
| Chain | Residue |
| A | TYR30 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue LI A 311 |
| Chain | Residue |
| A | ASN80 |
| A | HIS82 |
| A | ASP117 |
| A | FON301 |
| A | 0FX302 |
| A | HOH425 |
| site_id | AD3 |
| Number of Residues | 16 |
| Details | binding site for residue TYD B 301 |
| Chain | Residue |
| B | HOH558 |
| B | ASN10 |
| B | HIS63 |
| B | LYS65 |
| B | PHE93 |
| B | GLN95 |
| B | TYR139 |
| B | HIS205 |
| B | PHE208 |
| B | ASN210 |
| B | HOH414 |
| B | HOH415 |
| B | HOH418 |
| B | HOH424 |
| B | HOH455 |
| B | HOH457 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| A | PHE213 |
| B | SER131 |
| B | GLY194 |
| B | ASN198 |
| B | ARG201 |
| B | HOH412 |
| B | HOH500 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | CYS64 |
| B | HIS110 |
| B | GLN115 |
| B | LEU116 |
| B | ASP117 |
| B | HOH512 |
| B | HOH530 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 304 |
| Chain | Residue |
| B | SER134 |
| B | GLY136 |
| B | ASP206 |
| B | HOH626 |
| B | HOH649 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue EP1 B 305 |
| Chain | Residue |
| B | ASP206 |
| B | ASP207 |
| B | PHE208 |
| B | ARG209 |
| B | HOH464 |
| B | HOH565 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 306 |
| Chain | Residue |
| B | VAL53 |
| B | TYR56 |
| B | HOH422 |
| B | HOH535 |
| B | HOH586 |
| B | HOH619 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue K B 307 |
| Chain | Residue |
| A | GLU111 |
| A | HOH648 |
| A | HOH658 |
| B | ASP74 |
| B | HOH470 |
| B | HOH538 |
| B | HOH553 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"28665588","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28665588","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5VYQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
