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 | 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 | 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 |