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 | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:28665588 |
Chain | Residue | Details |
A | HIS82 | |
B | HIS82 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28665588, ECO:0007744|PDB:5VYQ |
Chain | Residue | Details |
A | ASN10 | |
B | HIS63 | |
B | GLN66 | |
B | GLY91 | |
B | ASP113 | |
B | ASP117 | |
B | LYS176 | |
B | ASN210 | |
A | HIS63 | |
A | GLN66 | |
A | GLY91 | |
A | ASP113 | |
A | ASP117 | |
A | LYS176 | |
A | ASN210 | |
B | ASN10 |