2OGF
Crystal structure of protein MJ0408 from Methanococcus jannaschii, Pfam DUF372
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 2001118 | biological_process | tetrahydromethanopterin biosynthetic process |
| B | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 2001118 | biological_process | tetrahydromethanopterin biosynthetic process |
| C | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 2001118 | biological_process | tetrahydromethanopterin biosynthetic process |
| D | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 2001118 | biological_process | tetrahydromethanopterin biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 501 |
| Chain | Residue |
| D | LYS70 |
| D | ARG72 |
| D | ASN73 |
| D | HOH652 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 502 |
| Chain | Residue |
| B | LYS70 |
| B | ARG72 |
| B | ASN73 |
| D | HOH657 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE OXG D 601 |
| Chain | Residue |
| B | PHE13 |
| B | GLU25 |
| B | ILE28 |
| B | PRO62 |
| D | PHE34 |
| D | TYR111 |
| D | PRO112 |
| D | MSE114 |
| D | HOH613 |
| D | HOH661 |
| B | PHE9 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE OXG A 602 |
| Chain | Residue |
| A | PHE13 |
| A | GLU25 |
| A | ILE28 |
| A | PRO62 |
| A | HOH622 |
| C | TYR111 |
| C | PRO112 |
| C | MSE114 |
| D | HOH679 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OXG B 603 |
| Chain | Residue |
| B | PHE34 |
| B | TYR111 |
| B | PRO112 |
| B | MSE114 |
| B | HOH640 |
| D | PHE13 |
| D | GLU25 |
| D | ILE28 |
| D | PRO62 |
| D | HOH606 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE OXG A 604 |
| Chain | Residue |
| A | TYR111 |
| A | PRO112 |
| A | MSE114 |
| A | HOH620 |
| C | PHE9 |
| C | PHE13 |
| C | GLU25 |
| C | ILE28 |
| C | PRO62 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 701 |
| Chain | Residue |
| C | GLU48 |
| C | GLU51 |
| C | GLU55 |
| C | VAL69 |
| C | LYS70 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 702 |
| Chain | Residue |
| B | TYR45 |
| C | ARG2 |
| C | LYS59 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|Ref.4 |
| Chain | Residue | Details |
| A | GLU25 | |
| C | GLU25 | |
| C | MSE114 | |
| D | GLU25 | |
| D | MSE114 | |
| A | MSE114 | |
| B | GLU25 | |
| B | MSE114 |
