2DWC
Crystal structure of Probable phosphoribosylglycinamide formyl transferase from Pyrococcus horikoshii OT3 complexed with ADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0003824 | molecular_function | catalytic activity |
| B | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| 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 | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 601 |
| Chain | Residue |
| B | LYS378 |
| B | TYR382 |
| B | ARG385 |
| B | HOH982 |
| B | HOH1200 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 602 |
| Chain | Residue |
| A | ARG414 |
| A | TRP420 |
| A | HOH942 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 603 |
| Chain | Residue |
| B | TRP420 |
| B | HOH904 |
| B | HOH1004 |
| B | ARG414 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 604 |
| Chain | Residue |
| A | LYS378 |
| A | TYR382 |
| A | ARG385 |
| A | HOH1074 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP A 501 |
| Chain | Residue |
| A | ARG121 |
| A | HIS160 |
| A | LYS162 |
| A | GLU202 |
| A | GLU203 |
| A | HIS204 |
| A | ILE205 |
| A | PHE207 |
| A | GLU210 |
| A | GLN237 |
| A | PHE281 |
| A | ASN290 |
| A | GLU291 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP B 502 |
| Chain | Residue |
| B | ARG121 |
| B | HIS160 |
| B | LYS162 |
| B | GLU202 |
| B | GLU203 |
| B | HIS204 |
| B | ILE205 |
| B | PHE207 |
| B | GLU210 |
| B | GLN237 |
| B | PHE281 |
| B | ASN290 |
| B | GLU291 |
| B | HOH1003 |
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 |
