2CZG
Crystal structure of Probable phosphoribosylglycinamide formyl transferase (PH0318) from Pyrococcus horikoshii OT3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| A | 0016742 | molecular_function | hydroxymethyl-, formyl- and related transferase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0043815 | molecular_function | phosphoribosylglycinamide formyltransferase 2 activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| B | 0016742 | molecular_function | hydroxymethyl-, formyl- and related transferase activity |
| B | 0016874 | molecular_function | ligase activity |
| B | 0043815 | molecular_function | phosphoribosylglycinamide formyltransferase 2 activity |
| 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 434 |
| Chain | Residue |
| B | LYS378 |
| B | TYR382 |
| B | ARG385 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 435 |
| Chain | Residue |
| B | ARG414 |
| B | TRP420 |
| B | HOH506 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 434 |
| Chain | Residue |
| A | HOH520 |
| A | LYS378 |
| A | TYR382 |
| A | ARG385 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 435 |
| Chain | Residue |
| A | ARG414 |
| A | TRP420 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 436 |
| Chain | Residue |
| B | HIS120 |
| B | ARG121 |
| B | GLU122 |
| B | ARG123 |
| B | ILE164 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 437 |
| Chain | Residue |
| B | ARG121 |
| B | ASN290 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 438 |
| Chain | Residue |
| A | ARG40 |
| A | GOL436 |
| A | HOH447 |
| B | ARG40 |
| B | PRO309 |
| B | GLY310 |
| B | HOH457 |
| B | HOH513 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 436 |
| Chain | Residue |
| A | GLU37 |
| A | THR303 |
| A | LEU304 |
| A | HIS307 |
| A | PRO308 |
| A | PRO309 |
| A | GLY310 |
| A | PHE311 |
| A | SER312 |
| A | HOH516 |
| B | GOL438 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 437 |
| Chain | Residue |
| A | ASN370 |
| A | TRP393 |
| B | PRO308 |
| B | PHE337 |
| B | PRO338 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 439 |
| Chain | Residue |
| A | PRO308 |
| A | PRO327 |
| A | PHE337 |
| A | PRO338 |
| B | ASN370 |
| B | TRP393 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 438 |
| Chain | Residue |
| A | ASP220 |
| A | TRP330 |
| A | ARG335 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 440 |
| Chain | Residue |
| B | VAL226 |
| B | THR227 |
| B | PHE229 |
| B | LYS264 |
| B | GLY333 |
| B | TYR334 |
| B | ARG335 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 439 |
| Chain | Residue |
| A | THR227 |
| A | LYS264 |
| A | HOH518 |
| A | HOH523 |
| B | VAL2 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 441 |
| Chain | Residue |
| A | ARG62 |
| A | HOH476 |
| B | ARG62 |
| B | SER63 |
| B | TYR64 |
| B | ARG80 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 442 |
| Chain | Residue |
| A | ASN53 |
| A | GOL441 |
| B | THR15 |
| B | HIS61 |
| B | ARG62 |
| B | HOH523 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 440 |
| Chain | Residue |
| A | ARG358 |
| B | GLU10 |
| B | SER18 |
| B | GLN20 |
| B | HOH510 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 441 |
| Chain | Residue |
| A | ARG62 |
| A | SER63 |
| A | TYR64 |
| A | ARG80 |
| B | GOL442 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01643 |
| Chain | Residue | Details |
| A | GLU29 | |
| B | GLU279 | |
| B | GLU291 | |
| B | ASP298 | |
| B | LYS378 | |
| B | ARG385 | |
| A | GLU89 | |
| A | GLU279 | |
| A | GLU291 | |
| A | ASP298 | |
| A | LYS378 | |
| A | ARG385 | |
| B | GLU29 | |
| B | GLU89 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01643, ECO:0000269|Ref.3 |
| Chain | Residue | Details |
| A | ARG121 | |
| A | LYS162 | |
| A | GLU202 | |
| A | GLU210 | |
| B | ARG121 | |
| B | LYS162 | |
| B | GLU202 | |
| B | GLU210 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ez1 |
| Chain | Residue | Details |
| A | ASP298 | |
| A | ARG385 | |
| A | THR299 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ez1 |
| Chain | Residue | Details |
| B | ASP298 | |
| B | ARG385 | |
| B | THR299 |
