3IUB
Crystal structure of pantothenate synthetase from Mycobacterium tuberculosis in complex with 5-Methoxy-N-(5-methylpyridin-2-ylsulfonyl)-1H-indole-2-carboxamide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0000166 | molecular_function | nucleotide 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 | 4 |
| Details | BINDING SITE FOR RESIDUE EOH A 689 |
| Chain | Residue |
| A | HOH462 |
| A | HOH538 |
| A | HOH649 |
| A | EDO694 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EOH A 691 |
| Chain | Residue |
| A | ASN176 |
| A | HOH481 |
| A | HOH669 |
| B | ALA21 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 692 |
| Chain | Residue |
| A | MET109 |
| A | TYR110 |
| A | GLY113 |
| A | ARG115 |
| A | THR116 |
| A | THR117 |
| A | LYS145 |
| B | ASP174 |
| A | MET71 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 693 |
| Chain | Residue |
| A | GLU128 |
| A | ARG132 |
| A | HIS135 |
| A | HOH456 |
| A | HOH525 |
| A | HOH560 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 694 |
| Chain | Residue |
| A | PRO111 |
| A | ASP112 |
| A | HOH538 |
| A | EOH689 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 696 |
| Chain | Residue |
| A | PRO38 |
| A | MET40 |
| A | GLN72 |
| A | VAL142 |
| A | FG2302 |
| A | HOH438 |
| A | HOH499 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 698 |
| Chain | Residue |
| A | THR218 |
| A | HOH361 |
| B | HIS222 |
| B | THR225 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FG2 A 302 |
| Chain | Residue |
| A | PRO38 |
| A | THR39 |
| A | MET40 |
| A | HIS44 |
| A | GLY46 |
| A | HIS47 |
| A | TYR82 |
| A | LYS160 |
| A | ASP161 |
| A | GLN164 |
| A | PRO185 |
| A | THR186 |
| A | VAL187 |
| A | MET195 |
| A | HOH488 |
| A | HOH501 |
| A | HOH539 |
| A | HOH677 |
| A | HOH681 |
| A | EDO696 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FG2 A 303 |
| Chain | Residue |
| A | MET71 |
| A | LEU114 |
| A | PRO133 |
| A | THR134 |
| A | GLY138 |
| A | HOH457 |
| A | HOH505 |
| A | HOH526 |
| A | HOH545 |
| A | HOH615 |
| B | PHE6 |
| B | PRO8 |
| B | ALA26 |
| B | GLN119 |
| B | HOH523 |
| B | EDO699 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 690 |
| Chain | Residue |
| A | ASP174 |
| B | MET109 |
| B | TYR110 |
| B | GLY113 |
| B | ARG115 |
| B | THR116 |
| B | LYS145 |
| B | HOH470 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 695 |
| Chain | Residue |
| B | GLN72 |
| B | VAL142 |
| B | FG2302 |
| B | HOH310 |
| B | HOH524 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 697 |
| Chain | Residue |
| B | PRO243 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 699 |
| Chain | Residue |
| A | ARG115 |
| A | THR117 |
| A | FG2303 |
| B | GLN119 |
| B | PRO120 |
| B | HOH377 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 700 |
| Chain | Residue |
| B | GLU128 |
| B | ARG132 |
| B | HIS135 |
| B | HOH457 |
| B | HOH562 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 701 |
| Chain | Residue |
| B | LEU123 |
| B | GLN170 |
| B | GLY256 |
| B | GLY258 |
| B | HOH306 |
| B | HOH414 |
| B | HOH478 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 702 |
| Chain | Residue |
| B | TYR162 |
| B | LEU165 |
| B | VAL166 |
| B | ARG169 |
| B | HOH336 |
| B | HOH438 |
| B | HOH624 |
| site_id | BC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FG2 B 302 |
| Chain | Residue |
| B | PRO38 |
| B | THR39 |
| B | MET40 |
| B | HIS44 |
| B | GLY46 |
| B | HIS47 |
| B | LYS160 |
| B | ASP161 |
| B | GLN164 |
| B | PRO185 |
| B | THR186 |
| B | VAL187 |
| B | MET195 |
| B | HOH497 |
| B | HOH511 |
| B | HOH535 |
| B | HOH602 |
| B | HOH680 |
| B | EDO695 |
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 |
