Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004329 | molecular_function | formate-tetrahydrofolate ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006730 | biological_process | one-carbon metabolic process |
A | 0016874 | molecular_function | ligase activity |
A | 0035999 | biological_process | tetrahydrofolate interconversion |
B | 0004329 | molecular_function | formate-tetrahydrofolate ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006730 | biological_process | one-carbon metabolic process |
B | 0016874 | molecular_function | ligase activity |
B | 0035999 | biological_process | tetrahydrofolate interconversion |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 601 |
Chain | Residue |
A | LYS74 |
A | ARG97 |
A | GLY303 |
A | PHE304 |
A | AGS700 |
A | HOH814 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 603 |
Chain | Residue |
A | HOH736 |
A | SER44 |
A | ASP46 |
A | LYS256 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 604 |
Chain | Residue |
A | ARG175 |
A | ARG178 |
A | GLY537 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 605 |
Chain | Residue |
A | SER446 |
A | ARG505 |
A | ARG507 |
A | HOH626 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AGS A 700 |
Chain | Residue |
A | GLU72 |
A | GLY73 |
A | LYS74 |
A | THR75 |
A | THR76 |
A | GLY113 |
A | ASN382 |
A | ALA383 |
A | PHE384 |
A | PRO385 |
A | TRP412 |
A | SO4601 |
A | HOH791 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE TOE A 701 |
Chain | Residue |
A | ARG162 |
A | ILE164 |
A | GLU194 |
A | HOH789 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE TOE A 702 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 602 |
Chain | Residue |
B | ARG175 |
B | ARG178 |
B | MET533 |
B | GLY537 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 601 |
Chain | Residue |
B | LYS74 |
B | ARG97 |
B | GLY303 |
B | PHE304 |
site_id | BC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE AGS B 700 |
Chain | Residue |
B | GLU9 |
B | GLY71 |
B | GLU72 |
B | GLY73 |
B | LYS74 |
B | THR75 |
B | THR76 |
B | GLY113 |
B | ALA383 |
B | PHE384 |
B | TRP412 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MAE B 702 |
Chain | Residue |
B | SER44 |
B | LYS252 |
B | LYS256 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MAE B 703 |
Chain | Residue |
B | ARG162 |
B | ILE164 |
B | GLU194 |
B | HOH606 |
B | HOH622 |
Functional Information from PROSITE/UniProt
site_id | PS00721 |
Number of Residues | 11 |
Details | FTHFS_1 Formate--tetrahydrofolate ligase signature 1. GIKGGAAGGGY |
Chain | Residue | Details |
A | GLY106-TYR116 | |
site_id | PS00722 |
Number of Residues | 12 |
Details | FTHFS_2 Formate--tetrahydrofolate ligase signature 2. VATVRALKmHGG |
Chain | Residue | Details |
A | VAL331-GLY342 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | THR68 | |
B | THR68 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 385 |
Chain | Residue | Details |
A | LYS74 | electrostatic stabiliser |
A | THR76 | steric role |
A | ARG97 | electrostatic stabiliser |
A | LYS108 | electrostatic stabiliser |
A | ALA276 | electrostatic stabiliser |
A | PHE304 | electrostatic stabiliser |
A | PHE384 | activator |
A | LYS414 | activator |
site_id | MCSA2 |
Number of Residues | 8 |
Details | M-CSA 385 |
Chain | Residue | Details |
B | LYS74 | electrostatic stabiliser |
B | THR76 | steric role |
B | ARG97 | electrostatic stabiliser |
B | LYS108 | electrostatic stabiliser |
B | ALA276 | electrostatic stabiliser |
B | PHE304 | electrostatic stabiliser |
B | PHE384 | activator |
B | LYS414 | activator |