1N2B
Crystal Structure of a Pantothenate Synthetase from M. tuberculosis in complex with AMPCPP and pantoate, higher occupancy of pantoate and lower occupancy of AMPCPP in subunit A
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 MG A 901 |
| Chain | Residue |
| A | ASP161 |
| A | APC801 |
| A | HOH1122 |
| A | HOH1143 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 902 |
| Chain | Residue |
| B | APC802 |
| B | HOH917 |
| B | HOH929 |
| B | HOH1021 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 601 |
| Chain | Residue |
| A | PRO58 |
| A | ARG154 |
| A | ARG56 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE APC A 801 |
| Chain | Residue |
| A | MET40 |
| A | HIS44 |
| A | HIS47 |
| A | LEU50 |
| A | TYR82 |
| A | PHE157 |
| A | GLY158 |
| A | LYS160 |
| A | ASP161 |
| A | THR186 |
| A | VAL187 |
| A | MET195 |
| A | SER196 |
| A | SER197 |
| A | ARG198 |
| A | MG901 |
| A | PAF1001 |
| A | HOH1031 |
| A | HOH1143 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE APC B 802 |
| Chain | Residue |
| B | HIS44 |
| B | HIS47 |
| B | LEU50 |
| B | TYR82 |
| B | PHE157 |
| B | GLY158 |
| B | LYS160 |
| B | ASP161 |
| B | THR186 |
| B | VAL187 |
| B | MET195 |
| B | SER196 |
| B | SER197 |
| B | ARG198 |
| B | GOL503 |
| B | MG902 |
| B | HOH922 |
| B | HOH929 |
| B | HOH938 |
| B | HOH1042 |
| B | HOH1054 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PAF A 1001 |
| Chain | Residue |
| A | PRO38 |
| A | MET40 |
| A | GLN72 |
| A | VAL142 |
| A | PHE157 |
| A | GLN164 |
| A | APC801 |
| A | HOH1003 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 501 |
| Chain | Residue |
| A | MET109 |
| A | TYR110 |
| A | PRO111 |
| A | ASP112 |
| A | GLY113 |
| A | ARG115 |
| A | THR116 |
| A | LYS145 |
| B | ASP174 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 502 |
| Chain | Residue |
| A | ASP174 |
| B | MET109 |
| B | TYR110 |
| B | PRO111 |
| B | ASP112 |
| B | GLY113 |
| B | LEU114 |
| B | ARG115 |
| B | THR116 |
| B | LYS145 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 503 |
| Chain | Residue |
| B | GLN72 |
| B | VAL139 |
| B | VAL142 |
| B | GLN164 |
| B | APC802 |
| B | HOH971 |
| B | HOH1054 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EOH A 701 |
| Chain | Residue |
| A | MET40 |
| A | GLN72 |
| A | HIS135 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EOH B 702 |
| Chain | Residue |
| B | GLU126 |
| B | ARG253 |
| B | LEU257 |
| B | GLY258 |
| B | PRO259 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EOH B 703 |
| Chain | Residue |
| B | SER24 |
| B | ARG25 |
| B | ARG28 |
| B | VAL150 |
| B | ARG151 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EOH B 704 |
| Chain | Residue |
| B | HIS222 |
| B | THR225 |
| A | THR218 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EOH B 705 |
| Chain | Residue |
| B | LEU147 |
| B | ARG151 |
| B | PRO152 |
| B | ASP178 |
| B | VAL179 |
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 |
