4Q12
Crystal structure of a putative uncharacterized protein Rv3404c and likely sugar N-formyltransferase from Mycobacterium tuberculosis bound to uridine diphosphate
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 | 16 |
Details | BINDING SITE FOR RESIDUE UDP A 301 |
Chain | Residue |
A | ASN10 |
A | ASN210 |
A | HOH403 |
A | HOH406 |
A | HOH407 |
A | HOH413 |
A | HOH414 |
A | HOH459 |
A | HIS63 |
A | LYS65 |
A | PHE93 |
A | GLN95 |
A | SER135 |
A | TYR139 |
A | HIS205 |
A | PHE208 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 302 |
Chain | Residue |
A | SER131 |
A | GLY194 |
A | ASN198 |
A | ARG201 |
A | HOH450 |
B | LEU187 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 303 |
Chain | Residue |
A | ILE73 |
A | VAL76 |
A | ARG77 |
A | CYS78 |
A | GLU111 |
A | ILE112 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 304 |
Chain | Residue |
A | LEU7 |
A | SER32 |
A | CYS64 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 305 |
Chain | Residue |
A | GLN66 |
A | HIS110 |
A | GLN115 |
A | ASP117 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 306 |
Chain | Residue |
A | HOH463 |
site_id | AC7 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE UDP B 301 |
Chain | Residue |
B | ASN10 |
B | HIS63 |
B | LYS65 |
B | PHE93 |
B | GLN95 |
B | SER135 |
B | TYR139 |
B | HIS205 |
B | PHE208 |
B | ASN210 |
B | HOH405 |
B | HOH406 |
B | HOH407 |
B | HOH408 |
B | HOH412 |
B | HOH423 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 302 |
Chain | Residue |
B | ILE73 |
B | VAL76 |
B | ARG77 |
B | CYS78 |
B | GLU111 |
B | ILE112 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 303 |
Chain | Residue |
A | PHE213 |
B | SER131 |
B | GLY194 |
B | ASN198 |
B | ARG201 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 304 |
Chain | Residue |
B | SER32 |
B | VAL45 |
B | CYS64 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 305 |
Chain | Residue |
B | CYS64 |
B | GLN66 |
B | ASN80 |
B | HIS110 |
B | ILE112 |
B | GLN115 |
B | ASP117 |
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 | VAL81 | |
B | VAL81 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28665588, ECO:0007744|PDB:5VYQ |
Chain | Residue | Details |
A | ASP9 | |
B | PHE62 | |
B | LYS65 | |
B | ARG90 | |
B | ILE112 | |
B | LEU116 | |
B | LEU175 | |
B | ARG209 | |
A | PHE62 | |
A | LYS65 | |
A | ARG90 | |
A | ILE112 | |
A | LEU116 | |
A | LEU175 | |
A | ARG209 | |
B | ASP9 |