3O1L
Crystal structure of a formyltetrahydrofolate deformylase (PSPTO_4314) from Pseudomonas syringae pv. tomato str. DC3000 at 2.20 A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006164 | biological_process | purine nucleotide biosynthetic process |
A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
A | 0006730 | biological_process | one-carbon metabolic process |
A | 0008864 | molecular_function | formyltetrahydrofolate deformylase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0016787 | molecular_function | hydrolase activity |
B | 0006164 | biological_process | purine nucleotide biosynthetic process |
B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
B | 0006730 | biological_process | one-carbon metabolic process |
B | 0008864 | molecular_function | formyltetrahydrofolate deformylase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 300 |
Chain | Residue |
A | TYR-3 |
A | ASP12 |
A | ARG13 |
A | VAL14 |
A | ILE16 |
A | VAL17 |
A | HOH465 |
B | ILE31 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 302 |
Chain | Residue |
A | ARG13 |
A | GLU73 |
A | HOH443 |
A | GLN-1 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 304 |
Chain | Residue |
A | ASP77 |
A | ARG79 |
A | LEU273 |
A | VAL274 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 305 |
Chain | Residue |
A | HIS37 |
A | ASP39 |
A | HIS275 |
A | LYS278 |
A | HOH405 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 A 308 |
Chain | Residue |
A | ARG242 |
A | HOH356 |
A | HOH367 |
A | HOH493 |
A | HOH578 |
B | SER35 |
B | HIS36 |
B | ARG242 |
B | HOH361 |
B | HOH454 |
B | HOH495 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 309 |
Chain | Residue |
A | MSE172 |
A | HIS192 |
A | ALA201 |
A | LYS202 |
A | PRO203 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 311 |
Chain | Residue |
A | SER94 |
A | ASN122 |
A | HIS123 |
A | MSE172 |
A | GLN173 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 313 |
Chain | Residue |
A | ARG95 |
A | HIS123 |
A | GLN124 |
A | ASP125 |
A | HIS139 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 314 |
Chain | Residue |
A | PHE251 |
A | ASP254 |
B | MSE258 |
B | ARG262 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 316 |
Chain | Residue |
A | HIS-7 |
A | ARG13 |
A | SER42 |
A | GLY43 |
A | TRP44 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 301 |
Chain | Residue |
B | ALA9 |
B | ASP77 |
B | TRP78 |
B | ARG79 |
B | LEU273 |
B | HOH377 |
site_id | BC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL B 303 |
Chain | Residue |
A | TRP30 |
A | ILE31 |
B | ASP12 |
B | ARG13 |
B | VAL14 |
B | ILE16 |
B | VAL17 |
B | PHE45 |
B | HOH401 |
B | HOH418 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 306 |
Chain | Residue |
A | ALA18 |
A | LYS19 |
A | ASN22 |
B | ASN22 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 307 |
Chain | Residue |
B | TRP107 |
B | HIS108 |
B | ASP110 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 310 |
Chain | Residue |
B | SER94 |
B | ARG95 |
B | ASN122 |
B | HIS123 |
B | GLN173 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 312 |
Chain | Residue |
B | MSE172 |
B | HIS192 |
B | ALA201 |
B | LYS202 |
B | HOH487 |
site_id | BC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 315 |
Chain | Residue |
B | LEU60 |
B | ARG64 |
B | GLN85 |