3LE8
Crystal Structure of Mycobacterium Tuberculosis Pantothenate Synthetase at 1.70 Angstrom resolution in complex with 2-(2-((benzofuran-2-carboxamido)methyl)-5-methoxy-1H-indol-1-yl)acetic acid
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 | 20 |
Details | BINDING SITE FOR RESIDUE 2B5 A 301 |
Chain | Residue |
A | PRO38 |
A | LYS160 |
A | GLN164 |
A | PRO185 |
A | THR186 |
A | VAL187 |
A | MET195 |
A | SER196 |
A | SER197 |
A | HOH440 |
A | HOH462 |
A | THR39 |
A | HOH533 |
A | MET40 |
A | HIS44 |
A | GLY46 |
A | HIS47 |
A | LEU50 |
A | VAL143 |
A | PHE157 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 302 |
Chain | Residue |
A | MET109 |
A | TYR110 |
A | GLY113 |
A | LEU114 |
A | ARG115 |
A | THR116 |
A | THR117 |
A | LYS145 |
B | ASP174 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 303 |
Chain | Residue |
A | PRO111 |
A | ASP112 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 304 |
Chain | Residue |
A | MET71 |
A | LEU114 |
A | THR134 |
A | HOH627 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 305 |
Chain | Residue |
A | MET71 |
A | LEU114 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 306 |
Chain | Residue |
A | LEU252 |
A | HOH467 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EOH A 307 |
Chain | Residue |
A | ALA226 |
B | ALA208 |
B | ALA209 |
B | VAL211 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 308 |
Chain | Residue |
A | ASN176 |
A | HOH371 |
A | HOH506 |
site_id | AC9 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 2B5 B 301 |
Chain | Residue |
B | PRO38 |
B | THR39 |
B | MET40 |
B | HIS44 |
B | GLY46 |
B | HIS47 |
B | VAL143 |
B | PRO185 |
B | VAL187 |
B | MET195 |
B | SER196 |
B | HOH479 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 302 |
Chain | Residue |
A | LEU114 |
A | ARG115 |
A | THR117 |
B | GLN119 |
B | PRO120 |
B | GLY121 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 303 |
Chain | Residue |
A | ARG169 |
A | ALA173 |
B | ARG115 |
B | HOH391 |
B | HOH501 |
B | HOH530 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 304 |
Chain | Residue |
A | GLN148 |
A | ARG151 |
B | LEU147 |
B | GLN148 |
B | LEU177 |
B | ASP178 |
B | VAL179 |
B | HOH371 |
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 |