4G5Y
Crystal Structure of Mycobacterium tuberculosis Pantothenate synthetase in a ternary complex with ATP and N,N-DIMETHYLTHIOPHENE-3-SULFONAMIDE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004592 | molecular_function | pantoate-beta-alanine ligase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0015940 | biological_process | pantothenate biosynthetic process |
A | 0016874 | molecular_function | ligase activity |
A | 0019482 | biological_process | beta-alanine metabolic process |
A | 0030145 | molecular_function | manganese ion binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004592 | molecular_function | pantoate-beta-alanine ligase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0015940 | biological_process | pantothenate biosynthetic process |
B | 0016874 | molecular_function | ligase activity |
B | 0019482 | biological_process | beta-alanine metabolic process |
B | 0030145 | molecular_function | manganese ion binding |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE ATP A 401 |
Chain | Residue |
A | PRO38 |
A | ASP161 |
A | THR186 |
A | VAL187 |
A | MET195 |
A | SER196 |
A | SER197 |
A | ARG198 |
A | MG402 |
A | HOH513 |
A | HOH672 |
A | MET40 |
A | HOH674 |
A | HOH678 |
A | HOH679 |
A | HOH682 |
A | HIS44 |
A | GLY46 |
A | HIS47 |
A | TYR82 |
A | PHE157 |
A | GLY158 |
A | LYS160 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 402 |
Chain | Residue |
A | ASP161 |
A | ATP401 |
A | HOH672 |
A | HOH674 |
A | HOH682 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 0OC A 403 |
Chain | Residue |
A | PRO38 |
A | THR39 |
A | MET40 |
A | PHE67 |
A | ASN69 |
A | GLN72 |
A | VAL142 |
A | VAL143 |
A | LEU146 |
A | HOH507 |
A | HOH676 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 404 |
Chain | Residue |
A | MET109 |
A | TYR110 |
A | PRO111 |
A | ASP112 |
A | GLY113 |
A | ARG115 |
A | THR116 |
A | LYS145 |
B | ASP174 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EOH A 405 |
Chain | Residue |
A | LEU114 |
A | ARG115 |
A | THR117 |
A | HOH671 |
B | GLN119 |
B | PRO120 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EOH A 406 |
Chain | Residue |
A | THR218 |
B | HIS222 |
B | THR225 |
B | HOH520 |
site_id | AC7 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ATP B 401 |
Chain | Residue |
B | PRO38 |
B | MET40 |
B | HIS44 |
B | GLY46 |
B | HIS47 |
B | LEU50 |
B | PHE157 |
B | GLY158 |
B | LYS160 |
B | ASP161 |
B | THR186 |
B | VAL187 |
B | MET195 |
B | SER196 |
B | SER197 |
B | ARG198 |
B | MG402 |
B | GOL405 |
B | HOH662 |
B | HOH689 |
B | HOH690 |
B | HOH691 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 402 |
Chain | Residue |
B | ATP401 |
B | GOL405 |
B | HOH689 |
B | HOH690 |
B | HOH691 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 0OC B 403 |
Chain | Residue |
B | PRO38 |
B | PHE67 |
B | ASN69 |
B | VAL142 |
B | VAL143 |
B | LEU146 |
B | HOH522 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 0OC B 404 |
Chain | Residue |
B | HOH587 |
A | ALA226 |
B | ALA208 |
B | ALA209 |
B | ALA212 |
B | ALA241 |
B | ALA242 |
B | PRO243 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 405 |
Chain | Residue |
B | LYS160 |
B | SER196 |
B | ARG198 |
B | LEU280 |
B | ATP401 |
B | MG402 |
B | HOH504 |
B | HOH691 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EOH B 406 |
Chain | Residue |
B | GLY244 |
B | ALA246 |
B | ARG273 |
B | LEU274 |
B | GLY275 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EOH B 407 |
Chain | Residue |
A | ARG169 |
A | HOH613 |
B | ARG115 |
B | HOH612 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | HIS47 | |
B | HIS47 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16460002 |
Chain | Residue | Details |
A | MET40 | |
A | GLY158 | |
A | VAL187 | |
A | MET195 | |
B | MET40 | |
B | GLY158 | |
B | VAL187 | |
B | MET195 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: |
Chain | Residue | Details |
A | GLN72 | |
B | GLN164 | |
A | ASP88 | |
A | ASP89 | |
A | GLN92 | |
A | GLN164 | |
B | GLN72 | |
B | ASP88 | |
B | ASP89 | |
B | GLN92 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609 |
Chain | Residue | Details |
A | ALA2 | |
B | ALA2 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 229 |
Chain | Residue | Details |
A | MET40 | electrostatic stabiliser |
A | ARG198 | electrostatic stabiliser, hydrogen bond donor |
A | HIS44 | electrostatic stabiliser, hydrogen bond donor, van der waals interaction |
A | HIS47 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, van der waals interaction |
A | ASP88 | metal ligand |
A | ASP89 | metal ligand |
A | GLN92 | metal ligand |
A | LYS160 | electrostatic stabiliser |
A | SER196 | electrostatic stabiliser, hydrogen bond donor |
A | SER197 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 10 |
Details | M-CSA 229 |
Chain | Residue | Details |
B | MET40 | electrostatic stabiliser |
B | ARG198 | electrostatic stabiliser, hydrogen bond donor |
B | HIS44 | electrostatic stabiliser, hydrogen bond donor, van der waals interaction |
B | HIS47 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, van der waals interaction |
B | ASP88 | metal ligand |
B | ASP89 | metal ligand |
B | GLN92 | metal ligand |
B | LYS160 | electrostatic stabiliser |
B | SER196 | electrostatic stabiliser, hydrogen bond donor |
B | SER197 | electrostatic stabiliser, hydrogen bond donor |