2NM2
Crystal structure of dihydroneopterin aldolase from S. aureus in complex with (1S,2R)-neopterin at 1.50 Angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| A | 0006760 | biological_process | folic acid-containing compound metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0046656 | biological_process | folic acid biosynthetic process |
| B | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| B | 0006760 | biological_process | folic acid-containing compound metabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0046656 | biological_process | folic acid biosynthetic process |
| C | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| C | 0006760 | biological_process | folic acid-containing compound metabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| C | 0046656 | biological_process | folic acid biosynthetic process |
| D | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| D | 0006760 | biological_process | folic acid-containing compound metabolic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| D | 0046656 | biological_process | folic acid biosynthetic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:17331536, ECO:0000305|PubMed:9586996 |
| Chain | Residue | Details |
| A | LYS100 | |
| B | LYS100 | |
| C | LYS100 | |
| D | LYS100 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17331536, ECO:0000305|PubMed:9586996, ECO:0007744|PDB:2NM2 |
| Chain | Residue | Details |
| A | GLU22 | |
| D | GLU22 | |
| D | TYR54 | |
| D | LEU73 | |
| A | TYR54 | |
| A | LEU73 | |
| B | GLU22 | |
| B | TYR54 | |
| B | LEU73 | |
| C | GLU22 | |
| C | TYR54 | |
| C | LEU73 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dhn |
| Chain | Residue | Details |
| A | GLU22 | |
| A | LYS100 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dhn |
| Chain | Residue | Details |
| B | GLU22 | |
| B | LYS100 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dhn |
| Chain | Residue | Details |
| C | GLU22 | |
| C | LYS100 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dhn |
| Chain | Residue | Details |
| D | GLU22 | |
| D | LYS100 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 664 |
| Chain | Residue | Details |
| A | GLU22 | electrostatic stabiliser |
| A | LYS100 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 664 |
| Chain | Residue | Details |
| B | GLU22 | electrostatic stabiliser |
| B | LYS100 | proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 2 |
| Details | M-CSA 664 |
| Chain | Residue | Details |
| C | GLU22 | electrostatic stabiliser |
| C | LYS100 | proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 2 |
| Details | M-CSA 664 |
| Chain | Residue | Details |
| D | GLU22 | electrostatic stabiliser |
| D | LYS100 | proton acceptor, proton donor |
