1MOP
Crystal Structure of a Pantothenate Synthetase from M. tuberculosis
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 | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 601 |
Chain | Residue |
B | ARG56 |
B | ARG154 |
B | HOH877 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 602 |
Chain | Residue |
A | ARG56 |
A | PRO58 |
A | ARG154 |
A | HOH837 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 603 |
Chain | Residue |
B | SER196 |
B | SER197 |
B | HIS44 |
B | TYR82 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 604 |
Chain | Residue |
A | HIS44 |
A | HIS47 |
A | LYS160 |
A | SER196 |
A | SER197 |
A | HOH804 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 501 |
Chain | Residue |
B | PRO38 |
B | GLN72 |
B | VAL142 |
B | GLN164 |
B | HOH750 |
B | HOH924 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 502 |
Chain | Residue |
A | MET109 |
A | TYR110 |
A | PRO111 |
A | ASP112 |
A | GLY113 |
A | ARG115 |
A | THR116 |
A | LYS145 |
B | ASP174 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 503 |
Chain | Residue |
A | PRO38 |
A | MET40 |
A | GLN72 |
A | VAL142 |
A | GLN164 |
A | HOH708 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 504 |
Chain | Residue |
A | ASP78 |
A | ALA81 |
A | HOH745 |
A | HOH813 |
A | HOH817 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EOH B 701 |
Chain | Residue |
B | PRO122 |
B | GLU126 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EOH B 702 |
Chain | Residue |
B | GLY59 |
B | HOH822 |
B | HOH908 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EOH B 703 |
Chain | Residue |
B | HIS44 |
B | GLY46 |
B | THR186 |
B | VAL187 |
B | MET195 |
B | HOH782 |
B | HOH862 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EOH A 704 |
Chain | Residue |
A | ILE255 |
A | GLY256 |
A | HOH858 |
A | HOH876 |
site_id | BC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EOH A 705 |
Chain | Residue |
A | ARG52 |
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 |